Viral polymerase and modulation thereof

ABSTRACT

The present invention provides the tertiary structure of a Hepatitis B Virus (HBV) polymerase reverse transcriptase (rt) domain from which a variant HBV polymerase mutations associated with resistance to or having reduced sensitivity to an anti-viral drug have been mapped. The present invention further provides methods of identifying, designing and/or modifying agents capable of modulating the functional activity of the HBV polymerase based on the atomic co-ordinates provided by the tertiary structure. The present invention still further provides a method of modulating HBV polymerase functional activity and agents useful for same. The agents identified in accordance with the method of the present invention are particularly useful inter alia in the treatment and/or prophylaxis of infection by an HBV resistant to or exhibiting reduced sensitivity to an anti-viral drug. The agents may also have utility as diagnostic agents such as to distinguish between resistance mutations. Furthermore, the present invention enables responses of particular potential anti-viral drugs to be predicted. In addition, new targets within the polymerase have been identified.

CROSS-REFERENCE TO RELATED APPLICATIONS

This application is a continuation of International Patent Application No. PCT/AU2004/000781 filed Jun. 11, 2004, which published in English and designated the United States, and which claims priority to Australian Patent Application No. 2003902983 filed Jun. 13, 2003.

BACKGROUND OF THE INVENTION

1. Field of the Invention

The present invention provides the tertiary structure of a Hepatitis B Virus (HBV) polymerase reverse transcriptase (rt) domain from which a variant HBV polymerase mutations associated with resistance to or having reduced sensitivity to an anti-viral drug have been mapped. The present invention further provides methods of identifying, designing and/or modifying agents capable of modulating the functional activity of the HBV polymerase based on the atomic co-ordinates provided by the tertiary structure. The present invention still further provides a method of modulating HBV polymerase functional activity and agents useful for same. The agents identified in accordance with the method of the present invention are particularly useful inter alia in the treatment and/or prophylaxis of infection by an HBV resistant to or exhibiting reduced sensitivity to an anti-viral drug. The agents may also have utility as diagnostic agents such as to distinguish between resistance mutations. Furthermore, the present invention enables responses of particular potential anti-viral drugs to be predicted. In addition, new targets within the polymerase have been identified.

2. Description of the Prior Art

Bibliographic details of the publications referred to in this specification are also collected at the end of the description.

Reference to any prior art in this specification is not, and should not be taken as, an acknowledgment or any form of suggestion that this prior art forms part of the common general knowledge in any country.

HBV is the leading cause of chronic hepatitis throughout the world. Notwithstanding the availability of a safe and effective vaccine, the world prevalence of HBV has not declined significantly thus resulting in the need for selective anti-viral agents. HBV is a small, partially double-stranded DNA virus which replicates through an RNA intermediate. Most efforts to develop anti-HBV agents have been targeted to the viral DNA polymerase which possesses reverse transcriptase activity. Currently, the most promising anti-HBV agents are nucleoside analogs which interfere with viral DNA replication. Although earlier nucleoside analogs such as fialuridine (FIAU) have displayed unacceptable toxicities, newer analogs such as lamivudine (3TC/LMV), BMS-200,475 and Adefovir Dipivoxial (ADV) have demonstrated clinical utility. In particular, the use of LMV has generated considerable interest in the development of other L-enantiomeric nucleoside analogs for use against HBV.

To date, small molecules have been screened for activity against the HBV polymerase utilizing in vitro assays. Although such screening technology facilitates the preliminary identification of molecules exhibiting anti-viral activity, such technology provides no scope for rationally designing or modifying agents to bind to the polymerase of the virus in order to maximize its functional impact. Rational design requires a detailed knowledge of the tertiary structure of the polymerase and in particular the nucelotide binding pocket.

To date, a number of polymerase molecules have been crystallized Klenow fragment of Escherichia coli DNA polymerase I, HIV-1 reverse transcriptase and bacteriophage T7 RNA polymerase (Sawaya et al., Science 264: 1930-1935, 1994). Several groups have developed structural models of HBV polymerase based on homology with the human immunodeficiency virus (HIV) reverse transcriptase (Bartholomeusz et al., Viral Hepatitis reviews 4: 167-187, 1998; Allen et al., Hepatology 27(6): 1670-1677, 1998; Das et al., V. Virol. 75(10): 4771-4779, 2001; Sawaya, 1994, supra). HIV polymerase and the resulting HBV models are described as having a “right hand structure”. The palm subdomain (FIG. 1, 1) of all polymerases has significant amino acid homology. The two conserved aspartic acid residues of the YMDD motif (FIG. 2, 2) in the C domain form part of a β-turn (Rodgers et al., Proc. Natl. Acad. Sci. USA 92(4): 1222-1226, 1995). The conserved aspartic acid residue within the A domain (FIG. 1, 3) is in close proximity to the two aspartic acid residues in the β-turn and together they form part of the active site. In HIV, this active site is part of a cavity which is bordered on one side by an alpha helix which is comprised of the conserved amino acid residues of the Domain B. These amino acid residues of the α helix are positioned near the template strand of the bound template-primer and form part of the template grip of Domain B (103, 104, 105). Wrobel et al. (Proc. Natl. Acad. Sci. USA 95(2): 638-645, 1998) examined the genetic variability of a number of HIV strains compared to the X-ray crystal structure. They found the residues predicted to be external were highly variable and the functional/catalytic residues (especially in the predicted nucleotide binding pocket) were highly conserved between the different HIV strains.

In facilitating the design or modification of HBV polymerase modulatory agents, knowledge of the primary, and even secondary structure, of the amino acid sequence of the protein is insufficient. Rather, it is necessary to know the precise tertiary structure of the subject viral polymerase in order to determine the residues critical to functions such as template binding and dNTP binding. Accordingly, there is a need to elucidate the structure of HBV polymerases from HBV agents resistant to particular nucleoside analogs in order to facilitate both small molecule screening and rational drug design/modification for the purpose of modulating the activity of such polymerases and thereby providing agents for therapeutic and/or prophylactic use in conditions such as infections by HBV agents which have become unresponsive to anti-viral agents such as ADV.

Recently, LMV was approved to treat chronic HBV infection (Dienstag, et al., N. Engl. J. Med. 341: 1256-1263, 1999). LMV is a dideoxycytidine analog that is active against human immunodeficiency virus (HIV) and HBV (Coates, et al., Antimicrob. Agents Chemother. 36: 733-739, 1992; Doong, et al., Proc. Natl. Acad. Sci. USA 88: 8495-8499, 1991). It is also shown that LMV acts as a chain terminator against viral DNA synthesis (Zhu, et al., Antimicrob. Agents Chemother. 42: 1805-1810, 1998). However, prolonged LMV treatment results in the emergence of LMV-resistant HBV mutants in 17 to 46% of patients treated for one year and more than 50% of patients within two years of treatment (Allen et al., Hepatology 27: 1670-1677, 1998; Dienstag, et al., 1998, supra; Jarvis and Faulds, Drugs 58: 101-141, 1999; Liaw, et al., Hepatology 30: 567-572, 1999). The emergence of drug-resistant HBV emphasizes the need to develop other anti-viral agents and therapeutic strategies.

In HBV, LMV resistance has been well documented and is primarily associated with changes at rtM204I/V (C domain) in combination with rtL180M (B domain) of the HBV polymerase. A number of other amino acid changes in the HBV polymerase have also been selected during LMV treatment and also Famciclovir (FCV) treatment.

ADV resistance has been recently described in HBV infected patients and this has been confirmed in vitro. ADV resistance was associated with mutations at rtN236T (Domain D) +/−rtA181V/T (Domain B). The modeling of these mutations within the polymerase is described.

Entecavir (ETV) resistance has also been identified two patients. In the first patient, this was associated with mutations at rtA38E, rtT184G (B domain) and rtS202I (C domain) in addition to the LMV resistant mutations at rtM204V and rtL80M. Phenotypic anti-viral testing revealed reduced ETV susceptibility when both the rtT184G and rtS202I changes were combined with the LMV-R mutations. In the second patient, ETV resistant mutations at rtI169T (B Domain) and rtM250V (E Domain) as well as the LMV resistant mutations rtL180M, rtM204V and rtV173V/L were detected.

Furthermore, the tertiary structure of the rt domain of wild-type HBV polymerase has been elucidated. The elucidation of this unique tertiary structure enables the rational analysis, design and/or modification of agents for use in modulating the functional activity of this anti-viral agent resistant HBV polymerase. This rational design is based on mapping of particular mutations to the wild-type HBV polymerase structure. This enables identification of agents capable of interacting with any HBV polymerase from an HBV such as HBV resistant to or exhibiting reduced sensitivity to an anti-viral drug such as a nucleoside analog. The present invention further enables mapping to other areas of an anti-viral drug binding pockets. In addition, the model can be used to identify other regions that are useful targets for anti-viral agents.

SUMMARY OF THE INVENTION

Throughout this specification, unless the context requires otherwise, the word “comprise”, or variations such as “comprises” or “comprising”, will be understood to imply the inclusion of a stated element or integer or group of elements or integers but not the exclusion of any other element or integer or group of elements or integers.

Nucleotide and amino acid sequences are referred to by a sequence identifier number (SEQ ID NO:). The SEQ ID NOs: correspond numerically to the sequence identifiers <400>1 (SEQ ID NO:1), <400>2 (SEQ ID NO:2), etc. A summary of the sequence identifiers is provided in Table 1. A sequence listing is provided after the claims.

Specific mutations in an amino acid sequence are represented herein as “Xaa₁nXaa₂” where Xaa₁ is the original amino acid residue before mutation, n is the residue number and Xaa₂ is the mutant amino acid. The abbreviation “Xaa” may be the three letter or single letter (i.e. “X”) code. An “rt” before “Xaa₁nXaa₂” means “reverse transcriptase”. An “s” means an envelope gene. The amino acid residues for HBV DNA polymerase are numbered with the residue methionine in the motif Tyr Met Asp Asp (YMDD) being residue number 204 (Stuyver et al., Hepatology 33: 751-757, 2001). The amino acid residues for hepatitis B virus surface antigen are number according to Norder et al. (J. Gen. Virol. 74: 341-1348, 1993). Both single and three letter abbreviations are used to define amino acid residues and these are summarized in Table 2.

The present invention is predicated in part on the elucidation of the tertiary structure of the rt domain of wild-type HBV polymerase. The tertiary structure of the rt domain is defined by a data set of atomic co-ordinates presented in Table 6. This elucidated structure provides the molecular basis for mapping resistance to nucleoside analogs or other anti-viral agents and, therefore, permits the identification, screening, analysis, rational design and/or modification of agents which interact with a particular HBV polymerase and optionally modulate the functional activity of the HBV polymerase. These agents may be used inter alia as either agonists or antagonists in the therapy and prophylaxis of infection by an HBV resistant to or exhibiting reduced sensitivity to an anti-viral agent. They may also be used as diagnostic agents such as having a capacity to distinguish between variant HBV polymerases having different or similar resistances to anti-viral drugs.

Accordingly, one aspect of the present invention is directed to a data set of atomic co-ordinates from a reverse transcriptase (rt) domain of an HBV polymerase, wherein said atomic co-ordinates are as set forth in Table 6.

Another aspect of the present invention is directed to a method of identifying an agent capable of interacting with an HBV polymerase or a homolog, derivative, analog or fragment thereof and modulating at least one functional activity associated with said polymerase, said method comprising contacting said polymerase with an agent and assessing the degree of interactive complementarity of said agent with said polymerase.

In one preferred embodiment, mutations in an HBV polymerase are mapped to the wild-type rt domain mutant HBV polymerase and generally have at least one of the following characteristics:

-   (i) displays increased resistance to a nucleoside analog such as but     not limited to ADV, LMV, FCV, FTC, ETV, DAPD, TDF and DXG compared     to native HBV polymerase; -   (ii) comprises a mutation within a region selected from amino acid     residues 28-36, 39-45, 59-66, 69-70, 73-93, 167-184, 198-213,     230-241 and 245-257 or 4-10, 24-27, 46-58, 67-68, 71-72, 94-120,     165-166, 185-197, 214-227, 242-244 and 258-266 such as but not     limited to rtA21S, rtA38E, rtY54H, rtN76D, rtL91I, rtF122L, rtY124H,     rtT128N, rtQ130P, rtT184G, rtM204V/I, rtS202I, rtH248N, rtY252L,     rtS21A, rtN/S/T/I/V53D, rtY54H, rtS57P, rtL91I, rtS116P, rtL122F,     rtF122L, rtN124H, rtY124H, rtH126R, rtY126Q, rtT128N, rtP130Q,     rtD131N, rtV134D, rtY135C, rtY141Y/F, rtL145M, rtF151T/F, rtL180M,     rtA181T, rtS202G, rtI204V, rtK212R, rtL217R, rtS219A, rtI235I/M,     rtN236T, rtN238D, sP120T, sM125T, sS126T, sT127A, sT118R, sM133L/M,     sM133T, sF134V, sS143S/T, sD144A, sG145A, sW172Stop, sI195M, sS207R,     sY225Y/C, spacerL97I, spacerK115R, spacerH116L, spacerL128F,     spacerS137G, spacerR139G, spacerF142S, rtA97V, rtH126R, rtS135Y,     rtM204I, PreS1 N114D, PreS1 T115S, PreS2 F22L, PreS2 V39A, PreS2     P52L, sL89V, sT118A, sF161L, sE164D, sI195M, sI208T, PreS1 E86Q,     PreS1 N91K, PreS2 P41H, sQ30K, sP120T, sL176V, sV194F, rtS21A,     rtL122F, rtN124H, rtH126R, rtP130Q, rtD131N, rtY135C,     rtN/S/T/I/V53D, rtY126Q, rtS202G, rtI204V, rtI235I/M, sM125T,     sT127A, sT118R, sM133T, sF134V, sI195M, sS207R, sY225Y/C, rtG172E,     rtG174C, rtP177L, rtL180V, rtT184S, sR160N, sE164D, sF170L,     sL175L/S, sQ181E/G/Q, sC/W182Y/STOP, sW196L, sW196S, sW196STOP,     sM198I, sW199S, sS204T, sY206N, sS210K, sS210R, sL216STOP, sY255F,     rtL77L/F, rtL77L/M/V, rtL80I, rtL80V, rtH90N/H, rtS117S/Y,     rt125DELrt128, rtQ125K, rtQ125N, rtY126Q, rtL128L/M, rtT128A,     rtL132L/M, rtN134G, rtS137T, rtN139H, rtN139K, rtY141Y/STOP,     rtV/G142L, rtL147L/W, rtK149R, rtG153E, rtR153Q, rtW153S, rtW153Q,     rtF166L, rtI169L, rtF178F/L, rtI187L, rtI187I/V, rtV191I, rtV191V/I,     rtN202S, rtS202S/C, rtS202G, rtS213T, rtV/G214E, rtS219A, rtS219P,     rtN/Q238H, rtN/S/H238N/K, rtN/S/H/T238/T/A/S/L, rtR242R/K,     rtR242R/S, rtN248H, rtI253A, s118-207, s117-120DEL, sI68I/M,     sC69F/L, sL109I/L, sG112R, sS17T, sT118R, sK122R, sT123P, sT126S,     sT131N, sN131T, sM133K/M, sM133I, sY/F134S, sC139C/G, sK141E,     sD144E, sG145R, rtT128T/I, rtL82M, rtT135C, rtT150A, rtV163I,     rtT184S, rtA200V, rtF202V, rtS213T, rtQ215H, rtS219A, rtA222T,     rtI224S, rtL229M, rtL235I, rtN238S, rtS78T, rt116DEL122, rtI163V,     rtL180V, rtE8A, rtV23I, rtD31D/G, rtY53D, rtV58V/I, rtA/S21T,     rtV/I/N/S/T53D, rtV/I/N/S/T53Y, rtS/T/N/H/A54Y/H, PreS2 L11L/A,     PreS2 R17I, DEL PreS2 18-21, PreS2 T30A, PreS2 N54H, sT13T/A, PreS2     Q1V, PreS2 Q1M, rtH90D, rtL/F108L, rtL157L/M, rtA181V, rtV207I,     rtP109S, rtN/H/A/S/Q238K, s181M, sP214Q, sF83S, sL173F, sW199L,     sI126T, sK160R, sS174N, sA84V, sS210N, sC69STOP/C, sC76Y, si110V/I,     sY134N, sW172STOP/W,     K32M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     N33D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     P34S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     H35I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     T37W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P59S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     K60M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     F61P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     A62R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     V63A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     D83C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/deletion;     V84A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     S85T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     A86R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/YV/deletion;     Y89V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     H90I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     I/L91K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/deletion;     P177S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     F178P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     L179K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     L180K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     A181R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     Q183E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     F183P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     T184W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     Y203V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     M204F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     L235K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N236D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     T237W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P237S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     N238D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H238I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     A238R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     S239T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     Q238E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     K239M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     L247K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N248D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H248I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     F249P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     M250F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     G251H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/deletion; and     V251A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; and/or -   (iii) comprises the amino acid sequence set forth in SEQ ID NO:1 or     an amino acid sequence defining an HBV polymerase and having a     sequence which is at least 70% similar after optimal alignment to     SEQ ID NO:1.

The present invention further identifies the primary and second amino acid residues in the HBV polymerase involved in nucleoside or nucleotide analog binding. The primary residues are at position numbers 28-36, 39-45, 59-66, 69-70, 73-93, 167-184, 198-213, 230-241 and 245-257 (FIG. 16). The secondary residues are at position numbers 4-10, 24-27, 46-58, 67-68, 71-72, 94-120, 165-166, 185-197, 214-227, 242-244 and 258-266 (FIG. 16).

Accordingly, the present invention extends to any mutation within amino acid residues 28-36, 39-45, 59-66, 69-70, 73-93, 167-184, 198-213, 230-241 and 245-257 or 4-10, 24-27, 46-58, 67-68, 71-72, 94-120, 165-166, 185-197, 214-227, 242-244 and 258-266 which confer resistance or reduced sensitivity to any anti-viral drug such as a nucleoside or nucleotide analog.

One particularly exemplified HBV polymerase is resistant to ADV and is mapped to the tertiary structure of the wild-type HBV polymerase.

Another aspect of the present invention provides a computer-assisted method for identifying agents potentially able to bind to a domain of HBV polymerase and optionally modulate at least one functional activity of the HBV polymerase using a programmed computer comprising the steps of:

-   (a) inputting into the progammed computer data comprising the atomic     co-ordinates of an HBV polymerase having a mutation within a region     selected from amino acid residues 28-36, 39-45, 59-66, 69-70, 73-93,     167-184, 198-213, 230-241 and 245-257 or 4-10, 24-27, 46-58, 67-68,     71-72, 94-120, 165-166, 185-197, 214-227, 242-244 and 258-266 such     as but not limited to rtA21S, rtA38E, rtY54H, rtN76D, rtL91I,     rtF122L, rtY124H, rtT128N, rtQ130P, rtT184G, rtM204V/I, rtS202I,     rtH248N, rtY252L, rtS21A, rtN/S/T/I/V53D, rtY54H, rtS57P, rtL91I,     rtS116P, rtL122F, rtF122L, rtN124H, rtY124H, rtH126R, rtY126Q,     rtT128N, rtP130Q, rtD131N, rtV134D, rtY135C, rtY141Y/F, rtL145M,     rtF151T/F, rtL180M, rtA181T, rtS202G, rtI204V, rtK212R, rtL217R,     rtS219A, rtI235I/M, rtN236T, rtN238D, sP120T, sM125T, sS126T,     sT127A, sT118R, sM133L/M, sM133T, sF134V, sS143S/T, sD144A, sG145A,     sW172Stop, sI195M, sS207R, sY225Y/C, spacerL97I, spacerK115R,     spacerH116L, spacerL128F, spacerS137G, spacerR139G, spacerF142S,     rtA97V, rtH126R, rtS135Y, rtM204I, PreS1 N114D, PreS1 T115S, PreS2     F22L, PreS2 V39A, PreS2 P52L, sL89V, sT118A, sF161L, sE164D, sI195M,     sI208T, PreS1 E86Q, PreS1 N91K, PreS2 P41H, sQ30K, sP120T, sL176V,     sV194F, rtS21A, rtL122F, rtN124H, rtH126R, rtP130Q, rtD131N,     rtY135C, rtN/S/T/I/V53D, rtY126Q, rtS202G, rtI204V, rtI235I/M,     sM125T, sT127A, sT118R, sM133T, sF134V, sI195M, sS207R, sY225Y/C,     rtG172E, rtG174C, rtP177L, rtL180V, rtT184S, sR160N, sE164D, sF170L,     sL175L/S, sQ181E/G/Q, sC/W182Y/STOP, sW196L, sW196S, sW196STOP,     sM198I, sW199S, sS204T, sY206N, sS210K, sS210R, sL216STOP, sY255F,     rtL77L/F, rtL77L/M/V, rtL80I, rtL80V, rtH90N/H, rtS117S/Y,     rt125DELrt128, rtQ125K, rtQ125N, rtY126Q, rtL128L/M, rtT128A,     rtL132L/M, rtN134G, rtS137T, rtN139H, rtN139K, rtY141Y/STOP,     rtV/G142L, rtL147L/W, rtK149R, rtG153E, rtR153Q, rtW153S, rtW153Q,     rtF166L, rtI169L, rtF178F/L, rtI187L, rtI187I/V, rtV191I, rtV191V/I,     rtN202S, rtS202S/C, rtS202G, rtS213T, rtV/G214E, rtS219A, rtS219P,     rtN/Q238H, rtN/S/H238N/K, rtN/S/H/T238/T/A/S/L, rtR242R/K,     rtR242R/S, rtN248H, rtI253A, s118-207, s117-120DEL, sI68I/M,     sC69F/L, sL109I/L, sG112R, sS17T, sT118R, sK122R, sT123P, sT126S,     sT131N, sN131T, sM133K/M, sM133I, sY/F134S, sC139C/G, sK141E,     sD144E, sG145R, rtT128T/I, rtL82M, rtT135C, rtT150A, rtV163I,     rtT184S, rtA200V, rtF202V, rtS213T, rtQ215H, rtS219A, rtA222T,     rtI224S, rtL229M, rtL235I, rtN238S, rtS78T, rt116DEL122, rtI163V,     rtL180V, rtE8A, rtV23I, rtD31D/G, rtY53D, rtV58V/I, rtA/S21T,     rtV/I/N/S/T53D, rtV/I/N/S/T53Y, rtS/T/N/H/A54Y/H, PreS2 L11L/A,     PreS2 R171, DEL PreS2 18-21, PreS2 T30A, PreS2 N54H, sT13T/A, PreS2     Q1V, PreS2 Q1M, rtH90D, rtL/F108L, rtL157L/M, rtA181V, rtV207I,     rtP109S, rtN/H/A/S/Q238K, s181M, sP214Q, sF83S, sL173F, sW199L,     sI126T, sK160R, sS174N, sA84V, sS210N, sC69STOP/C, sC76Y, si110V/I,     sY134N, sW172STOP/W,     K32M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     N33D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     P34S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     H35I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     T37W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P59S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     K60M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     F61P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     A62R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     V63A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     D83C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/deletion;     V84A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     S85T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     A86R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/YV/deletion;     Y89V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     H90I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     I/L91K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/deletion;     P177S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     F178P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     L179K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     L180K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     A181R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     Q183E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     F183P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     T184W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     Y203V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     M204F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     L235K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N236D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     T237W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P237S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     N238D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H238I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     A238R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     S239T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     Q238E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     K239M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     L247K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N248D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H248I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     F249P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     M250F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     G251H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/deletion; and     V251A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; -   (b) generating, using computer methods, a set of atomic co-ordinates     of a structure that possesses stereochemical complementarity to the     atomic co-ordinates defined in (a) or a subset thereof, thereby     generating a criteria data set; -   (c) comprising, using the processor, the criteria data set to a     computer database of chemical structures; -   (d) selecting from the database, using computer methods, chemical     structures which are similar to a portion f said criteria data set;     and -   (e) outputting the selected chemical structures which are similar to     a portion of the criteria data set.

Preferably, the method further comprises the step of obtaining an agent with a chemical structure selected in steps (d) and (e) and testing the compound for the ability to modulate at least one functional activity of an HBV polymerase.

Yet another aspect of the present invention provides a computer or a software component thereof for producing a three-dimensional representation of a molecule or molecular complex, which comprises a three-dimensional representation of a homolog of the molecule or molecular complex, in which the homolog comprises a domain that has a root mean square deviation from the backbone atoms of the amino acids of not more than 1.5 Å, in which the computer comprises:

-   (a) a machine-readable data storage medium comprising a data storage     material encoded with machine-readable data, wherein the data     comprises the structure co-ordinates of an HBV polymerase having a     mutation within a region selected from amino acid residues 28-36,     39-45, 59-66, 69-70, 73-93, 167-184, 198-213, 230-241 and 245-257 or     4-10, 24-27, 46-58, 67-68, 71-72, 94-120, 165-166, 185-197, 214-227,     242-244 and 258-266 such as but not limited to rtA21S, rtA38E,     rtY54H, rtN76D, rtL91I, rtF122L, rtY124H, rtT128N, rtQ130P, rtT184G,     rtM204V/I, rtS202I, rtH248N, rtY252L, rtS21A, rtN/S/T/I/V53D,     rtY54H, rtS57P, rtL91I, rtS116P, rtL122F, rtF122L, rtN124H, rtY124H,     rtH126R, rtY126Q, rtT128N, rtP130Q, rtD131N, rtV134D, rtY135C,     rtY141Y/F, rtL145M, rtF151T/F, rtL180M, rtA181T, rtS202G, rtI204V,     rtK212R, rtL217R, rtS219A, rtI235I/M, rtN236T, rtN238D, sP120T,     sM125T, sS126T, sT127A, sT118R, sM133L/M, sM133T, sF134V, sS143S/T,     sD144A, sG145A, sW172Stop, sI195M, sS207R, sY225Y/C, spacerL97I,     spacerK115R, spacerH116L, spacerL128F, spacerS137G, spacerR139G,     spacerF142S, rtA97V, rtH126R, rtS135Y, rtM204I, PreS1 N114D, PreS1     T115S, PreS2 F22L, PreS2 V39A, PreS2 P52L, sL89V, sT118A, sF161L,     sE164D, sI195M, sI208T, PreS1 E86Q, PreS1 N91K, PreS2 P41H, sQ30K,     sP120T, sL176V, sV194F, rtS21A, rtL122F, rtN124H, rtH126R, rtP130Q,     rtD131N, rtY135C, rtN/S/T/I/V53D, rtY126Q, rtS202G, rtI204V,     rtI235I/M, sM125T, sT127A, sT118R, sM133T, sF134V, sI195M, sS207R,     sY225Y/C, rtG172E, rtG174C, rtP177L, rtL180V, rtT184S, sR160N,     sE164D, sF170L, sL175L/S, sQ181E/G/Q, sC/W182Y/STOP, sW196L, sW196S,     sW196STOP, sM198I, sW199S, sS204T, sY206N, sS210K, sS210R,     sL216STOP, sY255F, rtL77L/F, rtL77L/M/V, rtL80I, rtL80V, rtH90N/H,     rtS117S/Y, rt125DELrt128, rtQ125K, rtQ125N, rtY126Q, rtL128L/M,     rtT128A, rtL132L/M, rtN134G, rtS137T, rtN139H, rtN139K,     rtY141Y/STOP, rtV/G142L, rtL147L/W, rtK149R, rtG153E, rtR153Q,     rtW153S, rtW153Q, rtF166L, rtI169L, rtF178F/L, rtI187L, rtI187I/V,     rtV191I, rtV191V/I, rtN202S, rtS202S/C, rtS202G, rtS213T, rtV/G214E,     rtS219A, rtS219P, rtN/Q238H, rtN/S/H238N/K, rtN/S/H/T238/T/A/S/L,     rtR242R/K, rtR242R/S, rtN248H, rtI253A, s118-207, s117-120DEL,     sI68I/M, sC69F/L, sL109I/L, sG112R, sS17T, sT118R, sK122R, sT123P,     sT126S, sT131N, sN131T, sM133K/M, sM133I, sY/F134S, sC139C/G,     sK141E, sD144E, sG145R, rtT128T/I, rtL82M, rtT135C, rtT150A,     rtV163I, rtT184S, rtA200V, rtF202V, rtS213T, rtQ215H, rtS219A,     rtA222T, rtI224S, rtL229M, rtL235I, rtN238S, rtS78T, rt116DEL122,     rtI163V, rtL180V, rtE8A, rtV23I, rtD31D/G, rtY53D, rtV58V/I,     rtA/S21T, rtV/I/N/S/T53D, rtV/I/N/S/T53Y, rtS/T/N/H/A54Y/H, PreS2     L11L/A, PreS2 R171, DEL PreS2 18-21, PreS2 T30A, PreS2 N54H,     sT13T/A, PreS2 Q1V, PreS2 Q1M, rtH90D, rtL/F108L, rtL157L/M,     rtA181V, rtV207I, rtP109S, rtN/H/A/S/Q238K, s181M, sP214Q, sF83S,     sL173F, sW199L, sI126T, sK160R, sS174N, sA84V, sS210N, sC69STOP/C,     sC76Y, si110V/I, sY134N, sW172STOP/W,     K32M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     N33D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     P34S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     H35I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     T37W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P59S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     K60M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     F61P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     A62R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     V63A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     D83C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/deletion;     V84A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     S85T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     A86R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/YV/deletion;     Y89V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     H90I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     I/L91K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/deletion;     P177S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     F178P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     L179K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     L180K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     A181R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     Q183E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     F183P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     T184W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     Y203V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     M204F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     L235K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N236D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     T237W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P237S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     N238D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H238I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     A238R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     S239T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     Q238E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     K239M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     L247K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N248D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H248I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     F249P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     M250F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     G251H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/deletion; and     V251A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; -   (b) a working memory for storing instructions for processing the     machine-readable data; -   (c) a central-processing unit coupled to the working memory and to     the machine-readable data storage medium for processing the     machine-readable data into the three-dimensional representation; and -   (d) a display coupled to the central-processing unit for displaying     the three-dimensional representation.

In one embodiment, the three-dimensional representation is of an HBV polymerase rt defined by the set of structure co-ordinates set out in Table 6 or wherein the three-dimensional representation is of a homolog of the molecule or molecular complex, the homolog having a root mean square deviation from the backbone atoms of the amino acids of not more than 1.5 Å.

An additional aspect of the present invention provides a computer or a software component thereof for determining at least a portion of the structure co-ordinates corresponding to a three-dimensional structure of a molecule or molecular complex comprising an HBV polymerase rt in which the computer comprises:

-   (a) a machine-readable data storage medium comprising a data storage     material encoded with machine-readable data, in which the data     comprises at least a portion of the structural co-ordinates of an     HBV polymerase having a mutation within a region selected from amino     acid residues 28-36, 39-45, 59-66, 69-70, 73-93, 167-184, 198 213,     230-241 and 245-257 or 4-10, 24-27, 46-58, 67-68, 71-72, 94-120,     165-166, 185-197, 214-227, 242-244 and 258-266 such as but not     limited to rtA21S, rtA38E, rtY54H, rtN76D, rtL91I, rtF122L, rtY124H,     rtT128N, rtQ130P, rtT184G, rtM204V/I, rtS202I, rtH248N, rtY252L,     rtS21A, rtN/S/T/I/V53D, rtY54H, rtS57P, rtL91I, rtS116P, rtL122F,     rtF122L, rtN124H, rtY124H, rtH126R, rtY126Q, rtT128N, rtP130Q,     rtD131N, rtV134D, rtY135C, rtY141Y/F, rtL145M, rtF151T/F, rtL180M,     rtA181T, rtS202G, rtI204V, rtK212R, rtL217R, rtS219A, rtI235I/M,     rtN236T, rtN238D, sP120T, sM125T, sS126T, sT127A, sT118R, sM133L/M,     sM133T, sF134V, sS143S/T, sD144A, sG145A, sW172Stop, sI195M, sS207R,     sY225Y/C, spacerL97I, spacerK115R, spacerH116L, spacerL128F,     spacerS137G, spacerR139G, spacerF142S, rtA97V, rtH126R, rtS135Y,     rtM204I, PreS1 N114D, PreS1 T115S, PreS2 F22L, PreS2 V39A, PreS2     P52L, sL89V, sT118A, sF161L, sE164D, sI195M, sI208T, PreS1 E86Q,     PreS1 N91K, PreS2 P41H, sQ30K, sP120T, sL176V, sV194F, rtS21A,     rtL122F, rtN124H, rtH126R, rtP130Q, rtD131N, rtY135C,     rtN/S/T/I/V53D, rtY126Q, rtS202G, rtI204V, rtI235I/M, sM125T,     sT127A, sT118R, sM133T, sF134V, sI195M, sS207R, sY225Y/C, rtG172E,     rtG174C, rtP177L, rtL180V, rtT184S, sR160N, sE164D, sF170L,     sL175L/S, sQ181E/G/Q, sC/W182Y/STOP, sW196L, sW196S, sW196STOP,     sM198I, sW199S, sS204T, sY206N, sS210K, sS210R, sL216STOP, sY255F,     rtL77L/F, rtL77L/M/V, rtL80I, rtL80V, rtH90N/H, rtS117S/Y,     rt125DELrt128, rtQ125K, rtQ125N, rtY126Q, rtL128L/M, rtT128A,     rtL132L/M, rtN134G, rtS137T, rtN139H, rtN139K, rtY141Y/STOP,     rtV/G142L, rtL147L/W, rtK149R, rtG153E, rtR153Q, rtW153S, rtW153Q,     rtF166L, rtI169L, rtF178F/L, rtI187L, rtI187I/V, rtV191I, rtV191V/I,     rtN202S, rtS202S/C, rtS202G, rtS213T, rtV/G214E, rtS219A, rtS219P,     rtN/Q238H, rtN/S/H238N/K, rtN/S/H/T238/T/A/S/L, rtR242R/K,     rtR242R/S, rtN248H, rtI253A, s118-207, s117-120DEL, sI68I/M,     sC69F/L, sL109I/L, sG112R, sS17T, sT118R, sK122R, sT123P, sT126S,     sT131N, sN131T, sM133K/M, sM133I, sY/F134S, sC139C/G, sK141E,     sD144E, sG145R, rtT128T/I, rtL82M, rtT135C, rtT150A, rtV163I,     rtT184S, rtA200V, rtF202V, rtS213T, rtQ215H, rtS219A, rtA222T,     rtI224S, rtL229M, rtL235I, rtN238S, rtS78T, rt116DEL122, rtI163V,     rtL180V, rtE8A, rtV23I, rtD31D/G, rtY53D, rtV58V/I, rtA/S21T,     rtV/I/N/S/T53D, rtV/I/N/S/T53Y, rtS/T/N/H/A54Y/H, PreS2 L11L/A,     PreS2 R171, DEL PreS2 18-21, PreS2 T30A, PreS2 N54H, sT13T/A, PreS2     Q1V, PreS2 Q1M, rtH90D, rtL/F108L, rtL157L/M, rtA181V, rtV207I,     rtP109S, rtN/H/A/S/Q238K, s181M, sP214Q, sF83S, sL173F, sW199L,     sI126T, sK160R, sS174N, sA84V, sS210N, sC69STOP/C, sC76Y, si110V/I,     sY134N, sW172STOP/W,     K32M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     N33D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     P34S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     H35I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     T37W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P59S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     K60M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     F61P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     A62R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     V63A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     D83C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/deletion;     V84A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     S85T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     A86R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/YV/deletion;     Y89V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     H90I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     I/L91K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/deletion;     P177S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     F178P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     L179K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     L180K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     A181R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     Q183E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     F183P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     T184W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     Y203V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     M204F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     L235K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N236D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     T237W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P237S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     N238D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H238I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     A238R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     S239T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     Q238E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     K239M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     L247K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N248D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H248I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     F249P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     M250F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     G251H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/deletion; and     V251A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; -   (b) a machine-readable data storage medium comprising a data storage     material encoded with machine-readable data, wherein the data     comprises atomic co-ordinates of the molecule or molecular complex; -   (c) a working memory for storing instructions for processing the     machine-readable data of (a) and (b); -   (d) a central-processing unit coupled to the working memory and to     the machine-readable data storage medium of (a) and (b) for     performing a transformation of the machine readable data of (a) and     for processing the machine-readable data of (b) into structure     co-ordinates; and -   (e) a display coupled to the central-processing unit for displaying     the structure co-ordinates of the molecule or molecular complex.

Another aspect of the present invention provides a computer-assisted method for identifying agents potentially able to bind to a domain of HBV polymerase and optionally modulate at least one functional activity of the HBV polymerase using a programmed computer comprising the steps of:

-   (a) inputting into the progammed computer data comprising the atomic     co-ordinates of an HBV polymerase rt or fragment thereof at     positions 28-36, 39-45, 59-66, 69-70, 73-93, 167-184, 198-213,     230-241 and 245-257 and/or at position numbers 4-10, 24-27, 46-58,     67-68, 71-72, 94-120, 165-166, 185-197, 214-227, 242-244 and     258-266; -   (b) generating, using computer methods, a set of atomic co-ordinates     of a structure that possesses stereochemical complementarity to the     atomic co-ordinates defined in (a) or a subset thereof, thereby     generating a criteria data set; -   (c) comprising, using the processor, the criteria data set to a     computer database of chemical structures; -   (d) selecting from the database, using computer methods, chemical     structures which are similar to a portion f said criteria data set;     and -   (e) outputting the selected chemical structures which are similar to     a portion of the criteria data set.

In another aspect, the present invention contemplates identifying an agent capable of interacting with an HBV polymerase or fragment thereof and optionally down-regulating at least one functional activity associated with said HBV polymerase wherein said HBV polymerase has at least one of the following characteristics:

-   (i) displays increased resistance or decreased sensitivity to a     nucleoside analog such as ADV, LMV, FCV, FTC, ETV, TDF, DAPD and DXG     compared to native HBV polymerase; -   (ii) comprises a mutation within a region selected from amino acid     residues 28-36, 39-45, 59-66, 69-70, 73-93, 167-184, 198-213,     230-241 and 245-257 or 4-10, 24-27, 46-58, 67-68, 71-72, 94-120,     165-166, 185-197, 214-227, 242-244 and 258-266 such as but not     limited to rtA21S, rtA38E, rtY54H, rtN76D, rtL91I, rtF122L, rtY124H,     rtT128N, rtQ130P, rtT184G, rtM204V/I, rtS202I, rtH248N, rtY252L,     rtS21A, rtN/S/T/I/V53D, rtY54H, rtS57P, rtL91I, rtS116P, rtL122F,     rtF122L, rtN124H, rtY124H, rtH126R, rtY126Q, rtT128N, rtP130Q,     rtD131N, rtV134D, rtY135C, rtY141Y/F, rtL145M, rtF151T/F, rtL180M,     rtA181T, rtS202G, rtI204V, rtK212R, rtL217R, rtS219A, rtI235I/M,     rtN236T, rtN238D, sP120T, sM125T, sS126T, sT127A, sT118R, sM133L/M,     sM133T, sF134V, sS143S/T, sD144A, sG145A, sW172Stop, sI195M, sS207R,     sY225Y/C, spacerL97I, spacerK115R, spacerH116L, spacerL128F,     spacerS137G, spacerR139G, spacerF142S, rtA97V, rtH126R, rtS135Y,     rtM204I, PreS1 N114D, PreS1 T115S, PreS2 F22L, PreS2 V39A, PreS2     P52L, sL89V, sT118A, sF161L, sE164D, sI195M, sI208T, PreS1 E86Q,     PreS1 N91K, PreS2 P41H, sQ30K, sP120T, sL176V, sV194F, rtS21A,     rtL122F, rtN124H, rtH126R, rtP130Q, rtD131N, rtY135C,     rtN/S/T/I/V53D, rtY126Q, rtS202G, rtI204V, rtI235I/M, sM125T,     sT127A, sT118R, sM133T, sF134V, sI195M, sS207R, sY225Y/C, rtG172E,     rtG174C, rtP177L, rtL180V, rtT184S, sR160N, sE164D, sF170L,     sL175L/S, sQ181E/G/Q, sC/W182Y/STOP, sW196L, sW196S, sW196STOP,     sM198I, sW199S, sS204T, sY206N, sS210K, sS210R, sL216STOP, sY255F,     rtL77L/F, rtL77L/M/V, rtL801, rtL80V, rtH90N/H, rtS117S/Y,     rt125DELrt128, rtQ125K, rtQ125N, rtY126Q, rtL128L/M, rtT128A,     rtL132L/M, rtN134G, rtS137T, rtN139H, rtN139K, rtY141Y/STOP,     rtV/G142L, rtL147L/W, rtK149R, rtG153E, rtR153Q, rtW153S, rtW153Q,     rtF166L, rtI169L, rtF178F/L, rtI187L, rtI187I/V, rtV191I, rtV191V/I,     rtN202S, rtS202S/C, rtS202G, rtS213T, rtV/G214E, rtS219A, rtS219P,     rtN/Q238H, rtN/S/H238N/K, rtN/S/H/T238/T/A/S/L, rtR242R/K,     rtR242R/S, rtN248H, rtI253A, s118-207, s117-120DEL, sI68I/M,     sC69F/L, sL109I/L, sG112R, sS17T, sT118R, sK122R, sT123P, sT126S,     sT131N, sN131T, sM133K/M, sM133I, sY/F134S, sC139C/G, sK141E,     sD144E, sG145R, rtT128T/I, rtL82M, rtT135C, rtT150A, rtV163I,     rtT184S, rtA200V, rtF202V, rtS213T, rtQ215H, rtS219A, rtA222T,     rtI224S, rtL229M, rtL235I, rtN238S, rtS78T, rt116DEL122, rtI163V,     rtL180V, rtE8A, rtV23I, rtD31D/G, rtY53D, rtV58V/I, rtA/S21T,     rtV/I/N/S/T53D, rtV/I/N/S/T53Y, rtS/T/N/H/A54Y/H, PreS2 L11L/A,     PreS2 R171, DEL PreS2 18-21, PreS2 T30A, PreS2 N54H, sT13T/A, PreS2     Q1V, PreS2 Q1M, rtH90D, rtL/F108L, rtL157L/M, rtA181V, rtV207I,     rtP109S, rtN/H/A/S/Q238K, s181M, sP214Q, sF83S, sL173F, sW199L,     sI126T, sK160R, sS174N, sA84V, sS210N, sC69STOP/C, sC76Y, si110V/I,     sY134N, sW172STOP/W,     K32M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     N33D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     P34S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     H35I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     T37W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P59S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     K60M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     F61P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     A62R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     V63A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     D83C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/deletion;     V84A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     S85T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     A86R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/YV/deletion;     Y89V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     H901/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     I/L91K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/deletion;     P177S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     F178P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     L179K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     L180K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     A181R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     Q183E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     F183P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     T184W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     Y203V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     M204F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     L235K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N236D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     T237W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P237S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     N238D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H238I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     A238R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     S239T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     Q238E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     K239M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     L247K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N248D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H248I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     F249P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     M250F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     G251H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/deletion; and     V251A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; and/or -   (iii) comprises the amino acid sequence set forth in SEQ ID NO:1 or     an amino acid sequence defining an HBV polymerase and having a     sequence which is at least 70% similar after optimal alignment to     SEQ ID NO:1;     said method comprising contacting said HBV polymerase with an agent     to be tested and assessing the degree of interactive complementarity     of said agent with said HBV polymerase.

In a particularly preferred embodiment, the method of the present invention is directed to identification of agents, such as nucleoside analogs, which bind to the nucleotide binding pocket of the nucleoside-resistant HBV polymerase molecule, or other regions of the polymerase that alters polymerase activity and to agents so identified. These may be useful as either therapeutic agents or diagnostic agents. The present method further provides an ability to map resistance to other areas of the rt domain of the HBV polymerase.

Preferably, the agent can bind to the nucleotide binding pocket of the HBV polymerase.

In another preferred embodiment, the functional activity is measured by inhibition of replication of an HBV.

In yet another preferred embodiment, identifies three potential metal binding regions with clusters of histidine and cysteine residues within the HBV polymerase structure. These new binding sites may be involved in polymerase activity or associated functions such as RNA/DNA binding or strand transfer of the newly elongated strand.

A further aspect of this invention three additional metal binding sites within the HBV polymerase and is directed to identification of agents, which bind to the metal binding sites within the HBV polymerase molecule, that alters polymerase activity and to agents so identified. These may be useful as either therapeutic agents or diagnostic agents. The present method further provides an ability to map resistance to other areas of the rt domain of the HBV polymerase including these three metal binding sites.

A further aspect of the present invention relates to the use of agents identified utilizing the methods described herein to modulate wild-type or anti-viral drug-resistant HBV polymerase activity and, in particular, the use of these agents in the therapeutic and/or prophylactic treatment of HBV infection. Other agents which interact with the HBV polymerase are useful as diagnostic agents.

Yet another aspect of the present invention provides a method modulating at least one functional activity associated with an HBV polymerase, said method comprising introducing into said subject an effective amount of an agent, which agent is identified in accordance with the methods herein defined, for a time and under conditions sufficient for said agent to interact with said HBV polymerase molecule and to inhibit or reduce its activity.

Preferably, the agent inhibits replication of the HBV.

This aspect of the present invention should be understood to encompass both in vivo treatment as well as modulating the activity of HBV polymerase in in vitro culture systems. The latter may be of benefit, for example, when screening for agents with antagonistic activity toward the HBV polymerase.

In yet another aspect, the present invention relates to a method for the treatment and/or prophylaxis of HBV infection, said method comprising administering to said subject an effective amount of an agent capable of modulating the HBV polymerase of said HBV, which agent is identified in accordance with the methods herein defined, for a time and under conditions sufficient for said agent to interact with said HBV polymerase molecule and inhibit or reduce its activity.

In a preferred embodiment, the subject of the prophylactic or therapeutic treatment is a mammal and more preferably a human.

In another aspect, the present invention relates to the use of an agent capable of modulating at least one functional activity associated with an HBV polymerase, which agent is identified in accordance with the methods herein defined, in the manufacture of a medicament for the treatment and/or prophylaxis of infection of a subject by HBV.

Yet another aspect of the present invention relates to a pharmaceutical composition comprising an agent which inhibits or reduces the activity of an HBV polymerase. Such compositions generally further comprise one or more pharmaceutically acceptable carriers and/or diluents.

The present invention should also be understood to extend to the use of the three-dimensional structural co-ordinates of an HBV polymerase or a domain thereof in the analysis and/or elucidation of the nucleic acid replication mechanism of a HBV. The present invention further extends to the diagnostic, therapeutic and/or prophylactic developments derived therefrom.

The present invention should still further be understood to extend to any non-naturally occurring form of the HBV polymerase molecule. Examples of non-naturally occurring forms of the HBV polymerase molecule include inter alia crystallized forms of the molecules.

The present invention further enables predictions to be made on the likelihood or otherwise of an agent inhibiting an HBV polymerase from a particular isolate.

A summary of sequence identifiers used throughout the subject specification is provided in Table 1. TABLE 1 Summary of sequence identifiers SEQUENCE ID NO: DESCRIPTION 1 amino acid sequence of ADV resistant HBV polymerase 2 amino acid sequence of motif 1 from HBV (FIG. 3) 3 amino acid sequence of motif 1 from WHV (FIG. 3) 4 amino acid sequence of motif 1 from DHBV (FIG. 3) 5 amino acid sequence of motif 1 from HIV (FIG. 3) 6 amino acid sequence of motif 2 from HBV (FIG. 3) 7 amino acid sequence of motif 2 from WHV (FIG. 3) 8 amino acid sequence of motif 2 from DHBV (FIG. 3) 9 amino acid sequence of motif 2 from HIV (FIG. 3) 10 amino acid sequence of motif 2 from PV (FIG. 3) 11 amino acid sequence of motif 2 from HCV (FIG. 3) 12 amino acid sequence of motif 2 from DEN (FIG. 3) 13 amino acid sequence of motif 2 from BVDV (FIG. 3) 14 amino acid sequence of motif 2 from Sindbis (FIG. 3) 15 amino acid sequence of motif 2 from HBV (FIG. 3) 16 amino acid sequence of motif 2 from WHV (FIG. 3) 17 amino acid sequence of motif 2 from DHBV protein (FIG. 3) 18 amino acid sequence showing the primary and secondary mutative binding sites for nucleoside and nucleotide analogs

Single and three letter abbreviations used throughout the specification are provided in Table 2. TABLE 2 Single and three letter amino acid abbreviations THREE-LETTER ONE-LETTER AMINO ACID ABBREVIATION SYMBOL Alanine Ala A Arginine Arg R Asparagine Asn N Aspartic acid Asp D Cysteine Cys C Glutamine Gln Q Glutamic acid Glu E Glycine Gly G Histidine His H Isoleucine Ile I Leucine Leu L Lysine Lys K Methionine Met M Phenylalanine Phe F Proline Pro P Serine Ser S Threonine Thr T Tryptophan Trp W Tyrosine Tyr Y Valine Val V Any residue Xaa X

A list of abbreviations used herein is provided in Table 3. TABLE 3 Abbreviations ABBREVIATION DESCRIPTION 3TC (LMV); (−)-β-2′-deoxy-3′-thiacytidine ADV adefovir DAPD diaminopurine dioxolane DXG dioxolane guanine ETV entecavir FCV famciclovir FTC emtricitabine HBV hepatitis B virus TDF tenofovir disoproxil fumarate LMV lamividuine rt reverse transcriptase YMDD Tyr Met Asp Asp-a motif in the polymerase protein; where the Met residue is designated residue number 204 of the reverse transcriptase

BRIEF DESCRIPTION OF THE FIGURES

FIG. 1 is an alignment of HBV and HIV showing resistance mutations. A colored version of this Figure is available from the Applicant upon request.

FIG. 2 is a photomicrographic representation of the homology model of HBV polymerase showing domains based on HIV reverse transcriptase. The model was constructed based on the crystal structure 1RTD (Das et al., Journal of Virology 75: 4771-4779, 2001) and the alignment of the HBV and HIV polymerase proteins (FIG. 1). The structurally conserved domains are highlighted; Domains F (red), A (orange), B (yellow), C (green). D (white) and E (pink). The template and primer strands of DNA are shown in blue and green. The magnesium ions present in the catalytic site are shown in purple. Three proposed metal binding sites are shown in grey. A colored version of this Figure is available from the Applicant upon request.

FIG. 3 is a representation showing motifs F and G domains.

FIG. 4 is a structural representation showing the binding site of the HBV double mutant rtM204V/rtL180M with LMV bound. The mutation of residue 180 is proposed to alter the conformation of rtF188 and cause an unfavourable steric interaction with LMV. A colored version of this Figure is available from the Applicant upon request.

FIG. 5 is a structural representation showing the binding site of native HBV (green) and HBV mutant V173L (white) with LMV bound showing the proximity between rtL173 and rtF88 Mutation at position 173 rotates the aromatic ring of F88 causing it to encroach upon the binding pocket blocking the binding of LMV. A colored version of this Figure is available from the Applicant upon request.

FIG. 6 is a structural representation showing binding site model of native HBV with ADV and magnesium ions (purple) showing the proximity (3.4 Å) of residue rtN236 to S85 and the active site. A colored version of this Figure is available from the Applicant upon request.

FIG. 7 is a diagrammatic representation of a system used to carry out the instructions encoded by the storage medium.

FIG. 8 is a diagrammatic representation of a cross-section of a magnetic storage medium.

FIG. 9 is a diagrammatic representation of a cross-section of an optically readable data storage system.

FIG. 10 is a structural representation showing the leucine to isoleucine mutation at position 80 involved in LMV resistance. A colored version of this Figure is available from the Applicant upon request.

FIG. 11 is a structural representation showing the valine to leucine mutation at position 173 leading to LMV resistance. A colored version of this Figure is available from the Applicant upon request.

FIG. 12 is a structural representation showing the alanine to threonine mutation at position 181 leading to ADV resistance.

FIG. 13 is structural representation showing the asparagine to threonine mutation at position 236 leading to ADV resistance.

FIG. 14 is a structural representation showing the alanine to glutamic mutation at position 38 leading to entecavir resistance.

FIG. 15 is a structural representation showing the serine to isoleucine mutation at position 202 leading to entecavir resistance.

FIG. 16 is an alignment of amino acid sequence showing the primary and secondary mutative binding sites for nucleoside and nucleotide analogs.

FIG. 17 is a structural representation showing the proposed metal binding Site 1. Residues forming the site are rtE1, rtH12, rtH13, rtH160 and rtA162.

FIG. 18 is a structural representation showing the proposed metal binding Site 2. Residues forming the site are: rtC-9, rtH-6, rtH90, rtL93 and rtH234.

FIG. 19 is a structural representation showing proposed metal binding Site 3. Residues forming the site are: rtH197, rtC198, rtH216 and rtC213.

FIG. 20 is representation of Southern blot showing HBV replicative intermediates detected in cells treated with ADV (0, 0.1, 0.5, 1.0, 5.0 10 μM) or LMV (0, 0.001, 0.01, 0.1, 1, 10 μM).

DETAILED DESCRIPTION OF THE INVENTION

The present invention provides of the tertiary structure of an rt domain of the wild-type HBV polymerase. This structure demonstrates the molecular basis for resistance of the HBV polymerases to anti-viral agents and, therefore, permits the identification, screening, analysis, rational design and/or modification of agents for modulating the functional activity of HBV polymerases and in particular HBV polymerases resistant to one or more of ADV, LMV, FCV, FTC, ETV, TDF, DAPD or DXG or nucleoside/nucleotide analogues. These agents may be used inter alia as either agonists or antagonists in the therapy and prophylaxis of conditions involving replication of HBV infection. The agents may also be used for diagnostic purposes.

Before describing the present invention in detail, it is to be understood that unless otherwise indicated, the subject invention is not limited to specific formulations of agents, manufacturing methods, dosage regimens, or the like, as such may vary. It is also to be understood that the terminology used herein is for the purpose of describing particular embodiments only and is not intended to be limiting.

It must be noted that, as used in the subject specification, the singular forms “a”, “an” and “the” include plural aspects unless the context clearly dictates otherwise. Thus, for example, reference to “an agent” includes a single agent, as well as two or more agents; “a nucleoside analog” includes a single analog, as well as two or more analogs; reference to “an HBV variant” includes reference to two or more HBV variants; and so forth.

In describing and claiming the present invention, the following terminology is used in accordance with the definitions set forth below.

The terms “agent”, “compound”, “active ingredient”, “pharmacologically active agent”, “medicament”, “active” and “drug” are used interchangeably herein to refer to a chemical compound that induces a desired effect such as inhibiting viral replication by inhibiting HBV DNA polymerase activity or function. The terms also encompass pharmaceutically acceptable and pharmacologically active ingredients of those active agents specifically mentioned herein including but not limited to salts, esters, amides, pro-drugs, active metabolites, analogs and the like. When the terms “agents”, “compound”, “active ingredient”, “pharmacologically active agent”, “medicament”, “active” and “drug” are used, then it is to be understood that this includes the active agent per se as well as pharmaceutically acceptable, pharmacologically active salts, esters, amides, pro-drugs, metabolites, analogs, etc.

The present invention contemplates, therefore, compounds useful in inhibiting HBV DNA polymerase or interacting with HBV polymerase such as diagnostic agents. Reference to a “nucleoside analog such as ADV, LMV, FCV, FTC, ETV, TDF, DAPD and/or DXG including combinations of two or more analogs.

The terms “effective amount” and “therapeutically effective amount” of an agent as used herein mean a sufficient amount of the agent to provide the desired therapeutic or physiological effect of inhibiting HBV polymerase or for use as a diagnostic reagent. Furthermore, an “effective HBV-inhibiting amount” or “effective symptom-ameloriating amount” of an agent is a sufficient amount of the agent to directly or indirectly inhibit replication. Undesirable effects, e.g. side effects, are sometimes manifested along with the desired therapeutic effect; hence, a practitioner balances the potential benefits against the potential risks in determining what is an appropriate “effective amount”. The exact amount required will vary from subject to subject, depending on the species, age and general condition of the subject, mode of administration and the like. Thus, it may not be possible to specify an exact “effective amount”. However, an appropriate “effective amount” in any individual case may be determined by one of ordinary skill in the art using only routine experimentation.

By “pharmaceutically acceptable” carrier, excipient or diluent is meant a pharmaceutical vehicle comprised of a material that is not biologically or otherwise undesirable, i.e. the material may be administered to a subject along with the selected active agent without causing any or a substantial adverse reaction. Carriers may include excipients and other additives such as diluents, detergents, coloring agents, wetting or emusifying agents, pH buffering agents, preservatives, and the like.

Similarly, a “pharmacologically acceptable” salt, ester, emide, prodrug or derivative of a compound as provided herein is a salt, ester, amide, prodrug or derivative that this not biologically or otherwise undesirable.

The terms “treating” and “treatment” as used herein refer to reduction in severity and/or frequency of symptoms, elimination of symptoms and/or underlying cause, prevention of the occurrence of symptoms and/or their underlying cause, and improvement or remediation of damage in relation to HBV infection. Thus, for example, “treating” a patient involves prevention of HBV infection as well as treatment of a clinically HBV symptomatic individual by inhibiting HBV replication by inhibiting HBV polymerase. Thus, for example, the present method of “treating” a patient with HBV infection or with a propensity for one to develop encompasses both prevention of HBV infection as well as treating HBV infection or symptoms thereof. In any event, the present invention contemplates the treatment or prophylaxis of HBV infection.

“Patient” as used herein refers to an animal, preferably a mammal and more preferably a primate including a lower primate and even more preferably, a human who can benefit from the formulations and methods of the present invention. A patient regardless of whether a human or non-human animal may be referred to as an individual, subject, animal, host or recipient. The compounds and methods of the present invention have applications in human medicine, veterinary medicine as well as in general, domestic or wild animal husbandry. For convenience, an “animal” includes an avian species such as a poultry bird (including ducks, chicken, turkeys and geese), an aviary bird or game bird. The condition in a non-human animal may not be a naturally occurring HBV infection but HBV-like infection may be induced.

As indicated above, the preferred animals are humans, non-human primates such as marmossets, baboons, orangutangs, lower primates such as tupia, livestock animals, laboratory test animals, companion animals or captive wild animals. A human is the most preferred target. However, non-human animal models may be used.

Examples of laboratory test animals include mice, rats, rabbits, guinea pigs and hamsters. Rabbits and rodent animals, such as rats and mice, provide a convenient test system or animal model as do primates and lower primates. Livestock animals include sheep, cows, pigs, goats, horses and donkeys. Non-mammalian animals such as avian species, zebrafish, amphibians (including cane toads) and Drosophila species such as Drosophila melanogaster are also contemplated. Instead of a live animal model, a test system may also comprise a tissue culture system.

HBV is a member of the Hepdnaviridae that includes also avian hepatitis viruses such as Duck hepatitis B virus (DHBV) and hepatitis viruses from mammals such as woodchuck hepatitis virus (WHV). These viruses have similarity to HBV and may be used in in vitro and in vivo or animal model systems to investigate HBV polymerases having resistance or reduced sensitivity to an anti-viral drug such as a nucleoside or nucleotide analog.

An “anti-HBV drug” includes a nucleoside or nucleotide analog, protein or chemical compound.

The present invention is directed to a method of identifying an agent capable of interacting with an HBV polymerase and preferably modulating at least one functional activity associated with said HBV polymerase, said method comprising contacting said HBV polymerase with an agent to be tested and assessing the degree of interactive complementarity of said agent with said polymerase.

The HBV polymerase may also be referred to as “pol”. The largest open reading frame (ORF) in the HBV genome encodes for the HBV polymerase. The pol is 90 kd in size and has RNA and DNA dependant polymerase activity (Toh, et al., Nature 305: 827-829, 1983). Pol plays a key role in HBV genome generation as well as pgRNA encapsidation. Pol is packaged together with pgRNA within HBV nucleocapsids (Mack et al., J. Virol. 62: 4786-4790, 1988).

The HBV polymerase has been divided into four characterized domains. Based on sequence homologies and studies on the mechanism of viral genome replication, most parts of pol are indispensable. The N-terminus portion of the protein acts in priming (−) DNA strand synthesis and ends up covalently linked to the 5′ end of the (−) DNA strand. This domain is termed terminal protein The subsequent domain does not appear to have any enzymatic function, but acts as a spacer between the first and third domains. The third domain has the reverse transcriptase functions. It occupies approximately 40% of the protein and exhibits the RNA and DNA dependent polymerase activity (Lanford et al., J. Virol. 73: 1885-1893, 1999). However, pol also requires the presence of metal ions and the presence of the stem loop for polymerase/rt activity to occur (Urban et al., J. Gen. Virol. 79: 1121-1131, 1998; Bartenschlager and Schaller, EMBO J. 7: 4185-4192, 1992; Tavis et al., J. Virol. 72: 5789-5796, 1998). The fourth domain of possesses its RNase H activity (Chang et al., Proc. Natl. Acad. Sci. USA 87: 5158-5162, 1990; Radziwill et al., J. Virol. 64: 613-620, 1990). This domain also plays a key role in HBV genome replication.

HBV polymerase also contains a number of regions that are homologous to other RNA dependent polymerases (Poch et al., European Molecular Biology Organisation 8: 3867-3874, 1989; Lesburg et al., Nat. Struct. Biol. 6(10): 937-943, 1999). These regions have been designated Domains A-G, where the recently designated Domains F and G are prior to Domain A in the deduced protein sequence (Lesburg, 1999, supra). Domain F was previously called motif 2 and Domain G was motif 1 in other reverse transcriptase proteins (Nakamura et al., Science 277: 955-959, 1997; Xiong and Eickbush, EMBO J. 9(10): 3353-3362, 1990). A general numbering system has been developed by Stuyver et al., 2001, supra, to provide uniformity in the numbering system of the amino acids for the HBV polymerase protein. In this system, the methionine in the YMDD motif (using single amino acid nomenclature) has been assigned to be residue 204 (formerly codon 539, 550 or 552; Table 4). In addition each of the four functional regions of the polymerase (terminal protein, spacer, reverse transcriptase and RNase H) are individually numbered. TABLE 4 Accepted domain-specific numbering system for HBV polymerase, RT domain, modified from Stuyver et al., 2001, supra HBV Gen- 1^(st) amino acid B domain B LMV- C domain LMV- o- rt domain associated mutation associated mutation type Previously New Previously New Previously New A 349 rt1 L528M rtL180M M552I/V rtM204I/V B/C/ 347 rt1 L526M rtL180M M550I/V rtM204I/V F/H D 336 rt1 L515M rtL180M M539I/V rtM204I/V E/G 346 rt1 L525M rtL180M M549I/V rtM204I/V

Anti-viral drugs contemplated by the present invention to which an HBV polymerase may become resistant comprise, but are in no way limited, to nucleoside analog drugs such as ADV, LMV, FCV, FTC, ETV, TDF, DAPD and DXG.

Non-limiting examples of methods of assessing activity of a drug which acts on an HBV polymerase including assessing the level of resistance to a drug include:

assessment of the clinical activity of the anti-viral agent in a patient infected with HBV;

the ability of the anti-viral agent to inhibit the replication of a virus in cell culture;

the in vitro measurement of the Km value between the anti-viral agent and the viral polymerase (Das et al., 2001, supra); and

the interaction between the anti-viral agent and viral polymerase using in-silico modeling (Das et al., 2001, supra).

An HBV polymerase resistant to an anti-viral agent includes an HBV polymerase which maintains functional activity in the presence of anti-viral drugs. Preferred anti-viral drugs are nucleoside analogs such as ADV, LMV, FCV, FTC, ETV, TDF, DAPD and DXG. For the purposes of the present invention, the term “native HBV polymerase” is to be understood as an HBV polymerases which is sensitive to inactivation by a nucleoside analog.

Nucleoside reverse transcriptase inhibitors (NRTIs) are also examples of nucleoside analogs or dideoxynucleoside analogs due to the absence of a 3′-hydroxyl group on the ribose moiety. As with endogenous nucleosides, the nucleoside analogs must be triphosphorylated into a nucleotide. Initially, the nucleoside analog biotransformation requires enzymes such as thymidine kinase, deoxycytidine kinase or inosine phosphotransferase to form the monophosphate metabolite. Once in the triphosphorylated form, the dideoxynucleotide can compete with naturally occurring nucleotides for DNA incorporation. The dideoxynucleotide will bind onto reverse transcriptase and become incorporated into the elongating viral complement DNA (cDNA). The absence of the 3′-hydroxyl group on the ribose moiety of these nucleosides/nucleotides causes DNA elongation to terminate.

An anti-viral drug-resistant HBV polymerase generally comprises one or more of the following characteristics:

-   (i) displays increased resistance or decreased sensitivity to a     nucleoside analog such as ADV, LMV, FCV, FTC, ETV, TDF, DAPD and DXG     compared to native HBV polymerase; -   (ii) comprises a mutation selected from within a region selected     from amino acid residues 28-36, 39-45, 59-66, 69-70, 73-93, 167-184,     198-213, 230-241 and 245-257 or 4-10, 24-27, 46-58, 67-68, 71-72,     94-120, 165-166, 185-197, 214-227, 242-244 and 258-266 such as but     not limited to rtA21S, rtA38E, rtY54H, rtN76D, rtL91I, rtF122L,     rtY124H, rtT128N, rtQ130P, rtT184G, rtM204V/I, rtS202I, rtH248N,     rtY252L, rtS21A, rtN/S/T/I/V53D, rtY54H, rtS57P, rtL91I, rtS116P,     rtL122F, rtF122L, rtN124H, rtY124H, rtH126R, rtY126Q, rtT128N,     rtP130Q, rtD131N, rtV134D, rtY135C, rtY141Y/F, rtL145M, rtF151T/F,     rtL180M, rtA181T, rtS202G, rtI204V, rtK212R, rtL217R, rtS219A,     rtI235I/M, rtN236T, rtN238D, sP120T, sM125T, sS126T, sT127A, sT118R,     sM133L/M, sM133T, sF134V, sS143S/T, sD144A, sG145A, sW172Stop,     sI195M, sS207R, sY225Y/C, spacerL97I, spacerK115R, spacerH116L,     spacerL128F, spacerS137G, spacerR139G, spacerF142S, rtA97V, rtH126R,     rtS135Y, rtM204I, PreS1 N114D, PreS1 T115S, PreS2 F22L, PreS2 V39A,     PreS2 P52L, sL89V, sT118A, sF161L, sE164D, sI195M, sI208T, PreS1     E86Q, PreS1 N91K, PreS2 P41H, sQ30K, sP120T, sL176V, sV194F, rtS21A,     rtL122F, rtN124H, rtH126R, rtP130Q, rtD131N, rtY135C,     rtN/S/T/I/V53D, rtY126Q, rtS202G, rtI204V, rtI235I/M, sM125T,     sT127A, sT118R, sM133T, sF134V, sI195M, sS207R, sY225Y/C, rtG172E,     rtG174C, rtP177L, rtL180V, rtT184S, sR160N, sE164D, sF170L,     sL175L/S, sQ181E/G/Q, sC/W182Y/STOP, sW196L, sW196S, sW196STOP,     sM198I, sW199S, sS204T, sY206N, sS210K, sS210R, sL216STOP, sY255F,     rtL77L/F, rtL77L/M/V, rtL80I, rtL80V, rtH90N/H, rtS117S/Y,     rt125DELrt128, rtQ125K, rtQ125N, rtY126Q, rtL128L/M, rtT128A,     rtL132L/M, rtN134G, rtS137T, rtN139H, rtN139K, rtY141Y/STOP,     rtV/G142L, rtL147L/W, rtK149R, rtG153E, rtR153Q, rtW153S, rtW153Q,     rtF166L, rtI169L, rtF178F/L, rtI187L, rtI187I/V, rtV191I, rtV191V/I,     rtN202S, rtS202S/C, rtS202G, rtS213T, rtV/G214E, rtS219A, rtS219P,     rtN/Q238H, rtN/S/H238N/K, rtN/S/H/T238/T/A/S/L, rtR242R/K,     rtR242R/S, rtN248H, rtI253A, s118-207, s117-120DEL, sI68I/M,     sC69F/L, sL109I/L, sG112R, sS17T, sT118R, sK122R, sT123P, sT126S,     sT131N, sN131T, sM133K/M, sM133I, sY/F134S, sC139C/G, sK141E,     sD144E, sG145R, rtT128T/I, rtL82M, rtT135C, rtT150A, rtV163I,     rtT184S, rtA200V, rtF202V, rtS213T, rtQ215H, rtS219A, rtA222T,     rtI224S, rtL229M, rtL235I, rtN238S, rtS78T, rt116DEL122, rtI163V,     rtL180V, rtE8A, rtV23I, rtD31D/G, rtY53D, rtV58V/I, rtA/S21T,     rtV/I/N/S/T53D, rtV/I/N/S/T53Y, rtS/T/N/H/A54Y/H, PreS2 L11L/A,     PreS2 R171, DEL PreS2 18-21, PreS2 T30A, PreS2 N54H, sT13T/A, PreS2     Q1V, PreS2 Q1M, rtH90D, rtL/F108L, rtL157L/M, rtA181V, rtV207I,     rtP109S, rtN/H/A/S/Q238K, s181M, sP214Q, sF83S, sL173F, sW199L,     sI126T, sK160R, sS174N, sA84V, sS210N, sC69STOP/C, sC76Y, si110V/I,     sY134N, sW172STOP/W,     K32M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/V/L/deletion;     N33D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     P34S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     H35I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     T37W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P59S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     K60M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     F61P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     A62R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     V63A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     D83C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/deletion;     V84A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     S85T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     A86R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/YV/deletion;     Y89V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     H901/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     I/L91K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/deletion;     P177S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     F178P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     L179K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     L180K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     A181R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     Q183E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     F183P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     T184W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     Y203V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     M204F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     L235K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N236D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     T237W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P237S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     N238D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H238I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     A238R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     S239T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     Q238E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     K239M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     L247K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N248D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H248I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     F249P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     M250F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     G251H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/deletion; and     V251A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; and/or -   (iii) comprises the amino acid sequence set forth in SEQ ID NO:1 or     an amino acid sequence defining an HBV polymerase and having a     sequence which is at least 70% similar after optimal alignment to     SEQ ID NO:1.

Reference to “at least 70% similarity” includes 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98 or 100% similarity.

The atomic co-ordinates of the rt domain of wild-type HBV polymerase to which various mutants have been mapped are set forth in Table 6. The present invention extends to the co-ordinates of HBV polymerases resistant to any other drug such as a nucleoside or nucleotide analog.

A range of HBV polymerases are contemplated herein including a wild-type HBV polymerase as well as a variant polymerase such as those carrying a mutation within a region selected from amino acid residues 28-36, 39-45, 59-66, 69-70, 73-93, 167-184, 198-213, 230-241 and 245-257 or 4-10, 24-27, 46-58, 67-68, 71-72, 94-120, 165-166, 185-197, 214-227, 242-244 and 258-266 such as but not limited to rtA21S, rtA38E, rtY54H, rtN76D, rtL91I, rtF122L, rtY124H, rtT128N, rtQ130P, rtT184G, rtM204V/I, rtS202I, rtH248N, rtY252L, rtS21A, rtN/S/T/I/V53D, rtY54H, rtS57P, rtL91I, rtS116P, rtL122F, rtF122L, rtN124H, rtY124H, rtH126R, rtY126Q, rtT128N, rtP130Q, rtD131N, rtV134D, rtY135C, rtY141Y/F, rtL145M, rtF151T/F, rtL180M, rtA181T, rtS202G, rtI204V, rtK212R, rtL217R, rtS219A, rtI235I/M, rtN236T, rtN238D, sP120T, sM125T, sS126T, sT127A, sT118R, sM133L/M, sM133T, sF134V, sS143S/T, sD144A, sG145A, sW172Stop, sI195M, sS207R, sY225Y/C, spacerL97I, spacerK15R, spacerH116L, spacerL128F, spacerS137G, spacerR139G, spacerF142S, rtA97V, rtH126R, rtS135Y, rtM204I, PreS1 N114D, PreS1 T115S, PreS2 F22L, PreS2 V39A, PreS2 P52L, sL89V, sT118A, sF161L, sE164D, sI195M, sI208T, PreS1 E86Q, PreS1 N91K, PreS2 P41H, sQ30K, sP120T, sL176V, sV194F, rtS21A, rtL122F, rtN124H, rtH126R, rtP130Q, rtD131N, rtY135C, rtN/S/T/I/V53D, rtY126Q, rtS202G, rtI204V, rtI235I/M, sM125T, sT127A, sT118R, sM133T, sF134V, sI195M, sS207R, sY225Y/C, rtG172E, rtG174C, rtP177L, rtL180V, rtT184S, sR160N, sE164D, sF170L, sL175L/S, sQ181E/G/Q, sC/W182Y/STOP, sW196L, sW196S, sW196STOP, sM198I, sW199S, sS204T, sY206N, sS210K, sS210R, sL216STOP, sY255F, rtL77L/F, rtL77L/M/V, rtL80I, rtL80V, rtH90N/H, rtS117S/Y, rt125DELrt128, rtQ125K, rtQ125N, rtY126Q, rtL128L/M, rtT128A, rtL132L/M, rtN134G, rtS137T, rtN139H, rtN139K, rtY141Y/STOP, rtV/G142L, rtL147L/W, rtK149R, rtG153E, rtR153Q, rtW153S, rtW153Q, rtF166L, rtI169L, rtF178F/L, rtI187L, rtI187I/V, rtV191I, rtV191V/I, rtN202S, rtS202S/C, rtS202G, rtS213T, rtV/G214E, rtS219A, rtS219P, rtN/Q238H, rtN/S/H238N/K, rtN/S/H/T238/T/A/S/L, rtR242R/K, rtR242R/S, rtN248H, rtI253A, s118-207, s117-120DEL, sI68I/M, sC69F/L, sL109I/L, sG112R, sS17T, sT118R, sK122R, sT123P, sT126S, sT131N, sN131T, sM133K/M, sM133I, sY/F134S, sC139C/G, sK141E, sD144E, sG145R, rtT128T/I, rtL82M, rtT135C, rtT150A, rtV163I, rtT184S, rtA200V, rtF202V, rtS213T, rtQ215H, rtS219A, rtA222T, rtI224S, rtL229M, rtL235I, rtN238S, rtS78T, rt116DEL122, rtI163V, rtL180V, rtE8A, rtV23I, rtD31D/G, rtY53D, rtV58V/I, rtA/S21T, rtV/I/N/S/T53D, rtV/I/N/S/T53Y, rtS/T/N/H/A54Y/H, PreS2 L11L/A, PreS2 R171, DEL PreS2 18-21, PreS2 T30A, PreS2 N54H, sT13T/A, PreS2 Q1V, PreS2 Q1M, rtH90D, rtL/F108L, rtL157L/M, rtA181V, rtV207I, rtP109S, rtN/H/A/S/Q238K, s181M, sP214Q, sF83S, sL173F, sW199L, sI126T, sK160R, sS174N, sA84V, sS210N, sC69STOP/C, sC76Y, s110V/I, sY134N, sW172STOP/W, K32M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion; N33D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; P34S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; H35I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; T37W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion; P59S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; K60M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion; F61P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; A62R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion; V63A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; D83C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/deletion; V84A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; S85T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion; A86R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/YV/deletion; Y89V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion; H901/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; I/L91K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/deletion; P177S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; F178P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; L179K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; L180K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; A181R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion; Q183E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion; F183P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; T184W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion; Y203V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion; M204F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion; L235K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; N236D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; T237W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion; P237S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; N238D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; H238I/L/K/M/P/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; A238R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion; S239T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion; Q238E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion; K239M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion; L247K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; N248D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; H248I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; F249P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; M250F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion; G251H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/deletion; and/or V251A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion.

The present invention further identifies the primary and second amino acid residues in the HBV polymerase involved in nucleoside or nucleotide analog binding. The primary residues are at position numbers 28-36, 39-45, 59-66, 69-70, 73-93, 167-184, 198-213, 230-241 and 245-257. The secondary residues are at position numbers 4-10, 24-27, 46-58, 67-68, 71-72, 94-120, 165-166, 185-197, 214-227, 242-244 and 258-266.

The present invention further identifies three new potential metal binding sites. Polymerase molecules require metal ions for catalysis. In addition to the known metal binding region (residues 205 and 206 in our model) three regions are identified containing clusters of histidine and cysteine residues. The proposed metal binding Site 1 includes residues rtE1, rtH12, rtH13 rtH160 and rtA162. The proposed metal binding Site 2 includes residues rtC-9, rtH-6, rtH90, rtL93 and rtH234. The proposed metal binding Site 3 includes residues rtH197, rtC198, rtH216 and rtC213. These additional metal binding sites for the HBV polymerase have not been previously identified and may be targets for antiviral compounds.

It should be understood that the HBV polymerase of the present invention, which is contacted with the putative agent for evaluation of interactive complementarity, may be a naturally occurring form of the protein or it may be recombinantly or synthetically produced. However, it should also be understood that the subject protein may take the form of an image, such as an electron density map, molecular models (including, but not limited to, stick, ball and stick, space filling or surface representation models) or other digital or non-digital surface representation models or image, which facilitates the analysis of said HBV polymerase: agent interactions utilizing techniques and software which would be known to those of skill in the art. For example, interaction analyzes can be performed utilizing techniques such as Biacore real-time analysis of on and off-rates and dissociation constants for binding of ligands (Gardsvoll et al., J Biol. Chem. 274(53): 37995-38003, 1999; Hoyer-Hansen et al., FEBS Lett. 420(1): 79-85, 1997; Ploug, Biochemistry 37(47): 16494-16505, 1998; Ploug et al., Biochemistry 33(30): 8991-8997, 1994; Ploug et al., Biochemistry 34(39): 12524-12534, 1995; Ploug et al., Biochemistry 37(11): 3612-3622, 1998) and NMR perturbation studies (Stephens et al., Biochemistry 31:7572-7579, 1992).

Reference to “assessing the degree of interactive complementarity” of an agent with the subject HBV polymerase should be understood as a reference to elucidating any feature of interest including, but not limited to, the nature and/or degree of interaction between the subject HBV polymerase and an agent of interest. As detailed above, any suitable technique can be utilized. Such techniques would be known to the person of skill in the art. In terms of the nature of the subject interaction, it may be desirable to assess the types of interactive mechanisms which occur between specific residues of any given agent and those of the HBV polymerase (for example, peptide bonding or formation of hydrogen bonds, ionic bonds, van der Waals forces, etc.) and/or their relative strengths. It may also be desirable to assess the degree of interaction which occurs between an agent of interest and the subject HBV polymerase. For example, by analyzing the location of actual sites of interaction between the subject agent and HBV polymerase, it is possible to determine the quality of fit of the agent into any region of the HBV polymerase and the relative strength and stability of that binding interaction. This is of particular relevance to determining the nature and position of the binding of the agent. For example, where it is desirable to inhibit HBV polymerase activity, a nucleoside analog agent which binds to the nucleotide binding pocket could be designed or identified. Alternatively, an agent which interacts with the HBV polymerase such that it blocks or otherwise hinders (for example, sterically hinders or chemically or electrostatically repels) the binding of a nucleotide or the nucleic acid template to the HBV polymerase molecule may be identified. Accordingly, reference to “interacting” should be understood to include reference to an agent associating with one or more HBV binding regions for the purpose of inhibiting replication of HBV. In this regard, the form of association which is required in relation to inhibiting HBV polymerase activity may not involve the formation of any interactive bonding mechanism, as this is traditionally understood, but may involve a non-bonding mechanism such as the proximal location of a region of the agent relative to the subject binding region of the HBV polymerase, for example, to effect steric hindrance with respect to the binding of a nucleotide to the binding pocket. Where the interaction takes the form of hindrance or the creation of other replusive forces, this should nevertheless be understood as a form of “interaction” despite the lack of formation of any of the traditional forms of bonding mechanisms.

It should also be understood that the anti-viral drug-resistant HBV polymerase of the present invention, which is utilized either in a physical form or as an image, as discussed herein, to assess the interactive complementarity of a putative agent may be a naturally occurring form of the HBV polymerase or it may be a derivative, homolog, analog, mutant, fragment or equivalent thereof. As detailed in relation to the polymerase itself, the derivative, homolog, analog, mutant, fragment or equivalent thereof may also take either a physical or non-physical (such as an image) form.

Derivatives include fragments, parts, portions, variants and mimetics from any source including fusion proteins. Parts or fragments include, for example, active regions of the HBV polymerase molecule. This is of particular relevance, for example, if one is interested in analysing the nucleotide binding regions. For example, and without limiting the present invention in any way, the incoming nucleotide is thought to interact with residues present in the “palm” sub-domain of the HBV polymerase. In some circumstances, it may be useful to examine only the fragment of the HBV polymerase molecule comprising these binding regions. Accordingly, it may only be necessary to isolate, synthesize, produce or depict one or more HBV domains or parts of domains in isolation. The present invention should, therefore, be understood to extend to the use of any fragment, part or portion of the HBV polymerase molecule.

Derivatives may be derived from insertion, deletion or substitution of amino acids. Amino acid insertional derivatives include amino and/or carboxylic terminal fusions as well as intrasequence insertions of single or multiple amino acids. This may be of particular relevance where it is desirable to apply the method of the present invention to analyzing interactions between a putative agent and mutants, variants or mimetics of the HBV polymerase. Insertional amino acid sequence variants are those in which one or more amino acid residues are introduced into a predetermined site in the protein although random insertion is also possible with suitable screening of the resulting product. Deletional variants are characterized by the removal of one or more amino acids from the sequence. Substitutional amino acid variants are those in which at least one residue in the sequence has been removed and a different residue inserted in its place. An example of substitutional amino acid variants are conservative amino acid substitutions. Conservative amino acid substitutions typically include substitutions within the following groups: glycine and alanine; valine, isoleucine and leucine; aspartic acid and glutamic acid; asparagine and glutamine; serine and threonine; lysine and arginine; and phenylalanine and tyrosine. Additions to amino acid sequences include fusions with other peptides, polypeptides or proteins.

Equivalents of the HBV polymerase of the present invention should be understood as encompassing molecules such as chemical equivalents exhibiting any one or more of the structural features of said HBV polymerase and may be derived from any source such as being chemically synthesized, theoretically predicted or identified via screening processes such as natural product screening.

The derivatives also include fragments having particular regions or parts of the entire protein fused to peptides, polypeptides or other proteinaceous or non-proteinaceous molecules.

Reference to “homologs” should be understood as a reference to polymerases derived from other viruses or to other substantially similar molecules from viruses or splicing variants of the same molecule.

Analogs contemplated herein include, but are not limited to, modification to side chains, incorporating of unnatural amino acids and/or their derivatives during peptide, polypeptide or protein synthesis and the use of crosslinkers and other methods which impose conformational constraints on the proteinaceous molecules or their analogs. The study and use of anti-viral resistant HBV polymerase analogs may also be useful in relation to identifying, studying and/or modulating the activity of said polymerase mutants, variants or mimetics.

Examples of side chain modifications contemplated by the present invention include modifications of amino groups such as by reductive alkylation by reaction with an aldehyde followed by reduction with NaBH4; amidination with methylacetimidate; acylation with acetic anhydride; carbamoylation of amino groups with cyanate; trinitrobenzylation of amino groups with 2,4,6-trinitrobenzene sulphonic acid (TNBS); acylation of amino groups with succinic anhydride and tetrahydrophthalic anhydride; and pyridoxylation of lysine with pyridoxal-5-phosphate followed by reduction with NaBH4.

The guanidine group of arginine residues may be modified by the formation of heterocyclic condensation products with reagents such as 2,3-butanedione, phenylglyoxal and glyoxal.

The carboxyl group may be modified by carbodiimide activation via O-acylisourea formation followed by subsequent derivitization, for example, to a corresponding amide.

Sulphydryl groups may be modified by methods such as carboxymethylation with iodoacetic acid or iodoacetamide; performic acid oxidation to cysteic acid; formation of a mixed disulphides with other thiol compounds; reaction with maleimide, maleic anhydride or other substituted maleimide; formation of mercurial derivatives using 4-chloromercuribenzoate, 4-chloromercuriphenylsulphonic acid, phenylmercury chloride, 2-chloromercuri-4-nitrophenol and other mercurials; carbamoylation with cyanate at alkaline pH.

Tryptophan residues may be modified by, for example, oxidation with N-bromosuccinimide or alkylation of the indole ring with 2-hydroxy-5-nitrobenzyl bromide or sulphenyl halides. Tyrosine residues on the other hand, may be altered by nitration with tetranitromethane to form a 3-nitrotyrosine derivative.

Modification of the imidazole ring of a histidine residue may be accomplished by alkylation with iodoacetic acid derivatives or N-carboethoxylation with diethylpyrocarbonate.

Examples of incorporating unnatural amino acids and derivatives during protein synthesis include, but are not limited to, use of norleucine, 4-amino butyric acid, 4-amino-3-hydroxy-5-phenylpentanoic acid, 6-aminohexanoic acid, t-butylglycine, norvaline, phenylglycine, ornithine, sarcosine, 4-amino-3-hydroxy-6-methylheptanoic acid, 2-thienyl alanine and/or D-isomers of amino acids. A list of unnatural amino acids contemplated herein is shown in Table 5. TABLE 5 Codes for non-conventional amino acids Non-conventional Non-conventional amino acid Code amino acid Code α-aminobutyric acid Abu L-N-methylalanine Nmala α-amino-α-methylbutyrate Mgabu L-N-methylarginine Nmarg aminocyclopropane- Cpro L-N-methylasparagine Nmasn carboxylate L-N-methylaspartic acid Nmasp aminoisobutyric acid Aib L-N-methylcysteine Nmcys aminonorbornyl- Norb L-N-methylglutamine Nmgln carboxylate L-N-methylglutamic acid Nmglu cyclohexylalanine Chexa L-Nmethylhistidine Nmhis cyclopentylalanine Cpen L-N-methylisolleucine Nmile D-alanine Dal L-N-methylleucine Nmleu D-arginine Darg L-N-methyllysine Nmlys D-aspartic acid Dasp L-N-methylmethionine Nmmet D-cysteine Dcys L-N-methylnorleucine Nmnle D-glutamine Dgln L-N-methylnorvaline Nmnva D-glutamic acid Dglu L-N-methylornithine Nmorn D-histidine Dhis L-N-methylphenylalanine Nmphe D-isoleucine Dile L-N-methylproline Nmpro D-leucine Dleu L-N-methylserine Nmser D-lysine Dlys L-N-methylthreonine Nmthr D-methionine Dmet L-N-methyltryptophan Nmtrp D-ornithine Dorn L-N-methyltyrosine Nmtyr D-phenylalanine Dphe L-N-methylvaline Nmval D-proline Dpro L-N-methylethylglycine Nmetg D-serine Dser L-N-methyl-t-butylglycine Nmtbug D-threonine Dthr L-norleucine Nle D-tryptophan Dtrp L-norvaline Nva D-tyrosine Dtyr α-methyl-aminoisobutyrate Maib D-valine Dval α-methyl-γ-aminobutyrate Mgabu D-α-methylalanine Dmala α-methylcyclohexylalanine Mchexa D-α-methylarginine Dmarg α-methylcylcopentylalanine Mcpen D-α-methylasparagine Dmasn α-methyl-α-napthylalanine Manap D-α-methylaspartate Dmasp α-methylpenicillamine Mpen D-α-methylcysteine Dmcys N-(4-aminobutyl)glycine Nglu D-α-methylglutamine Dmgln N-(2-aminoethyl)glycine Naeg D-α-methylhistidine Dmhis N-(3-aminopropyl)glycine Norn D-α-methylisoleucine Dmile N-amino-α-methylbutyrate Nmaabu D-α-methylleucine Dmleu α-napthylalanine Anap D-α-methyllysine Dmlys N-benzylglycine Nphe D-α-methylmethionine Dmmet N-(2-carbamylethyl)glycine Ngln D-α-methylornithine Dmorn N-(carbamylmethyl)glycine Nasn D-α-methylphenylalanine Dmphe N-(2-carboxyethyl)glycine Nglu D-α-methylproline Dmpro N-(carboxymethyl)glycine Nasp D-α-methylserine Dmser N-cyclobutylglycine Ncbut D-α-methylthreonine Dmthr N-cycloheptylglycine Nchep D-α-methyltryptophan Dmtrp N-cyclohexylglycine Nchex D-α-methyltyrosine Dmty N-cyclodecylglycine Ncdec D-α-methylvaline Dmval N-cylcododecylglycine Ncdod D-N-methylalanine Dnmala N-cyclooctylglycine Ncoct D-N-methylarginine Dnmarg N-cyclopropylglycine Ncpro D-N-methylasparagine Dnmasn N-cycloundecylglycine Ncund D-N-methylaspartate Dnmasp N-(2,2-diphenylethyl)glycine Nbhm D-N-methylcysteine Dnmcys N-(3,3-diphenylpropyl)glycine Nbhe D-N-methylglutamine Dnmgln N-(3-guanidinopropyl)glycine Narg D-N-methylglutamate Dnmglu N-(1-hydroxyethyl)glycine Nthr D-N-methylhistidine Dnmhis N-(hydroxyethyl))glycine Nser D-N-methylisoleucine Dnmile N-(imidazolylethyl))glycine Nhis D-N-methylleucine Dnmleu N-(3-indolylyethyl)glycine Nhtrp D-N-methyllysine Dnmlys N-methyl-γ-aminobutyrate Nmgabu N-methylcyclohexylalanine Nmchexa D-N-methylmethionine Dnmmet D-N-methylornithine Dnmorn N-methylcyclopentylalanine Nmcpen N-methylglycine Nala D-N-methylphenylalanine Dnmphe N-methylaminoisobutyrate Nmaib D-N-methylproline Dnmpro N-(1-methylpropyl)glycine Nile D-N-methylserine Dnmser N-(2-methylpropyl)glycine Nleu D-N-methylthreonine Dnmthr D-N-methyltryptophan Dnmtrp N-(1-methylethyl)glycine Nval D-N-methyltyrosine Dnmtyr N-methyla-napthylalanine Nmanap D-N-methylvaline Dnmval N-methylpenicillamine Nmpen γ-aminobutyric acid Gabu N-(p-hydroxyphenyl)glycine Nhtyr L-t-butylglycine Tbug N-(thiomethyl)glycine Ncys L-ethylglycine Etg penicillamine Pen L-homophenylalanine Hphe L-α-methylalanine Mala L-α-methylarginine Marg L-α-methylasparagine Masn L-α-methylaspartate Masp L-α-methyl-t-butylglycine Mtbug L-α-methylcysteine Mcys L-methylethylglycine Metg L-α-methylglutamine Mgln L-α-methylglutamate Mglu L-α-methylhistidine Mhis L-α-methylhomophenylalanine Mhphe L-α-methylisoleucine Mile N-(2-methylthioethyl)glycine Nmet L-α-methylleucine Mleu L-α-methyllysine Mlys L-α-methylmethionine Mmet L-α-methylnorleucine Mnle L-α-methylnorvaline Mnva L-α-methylornithine Morn L-α-methylphenylalanine Mphe L-α-methylproline Mpro L-α-methylserine Mser L-α-methylthreonine Mthr L-α-methyltryptophan Mtrp L-α-methyltyrosine Mtyr L-α-methylvaline Mval L-N-methylhomophenylalanine Nmhphe N-(N-(2,2-diphenylethyl) Nnbhm N-(N-(3,3-diphenylpropyl) Nnbhe carbamylmethyl)glycine carbamylmethyl)glycine 1-carboxy-1-(2,2-diphenyl- Nmbc ethylamino)cyclopropane

Crosslinkers can be used, for example, to stabilize 3D conformations, using homo-bifunctional crosslinkers such as the bifunctional imido esters having (CH₂)_(n) spacer groups with n=1 to n=6, glutaraldehyde, N-hydroxysuccinimide esters and hetero-bifunctional reagents which usually contain an amino-reactive moiety such as N-hydroxysuccinimide and another group specific-reactive moiety.

Elucidation of the three dimensional structure of the HBV polymerase molecule facilitates the identification and analysis of regions involved in the binding between the HBV polymerase and anti-viral drugs. Examples of anti-viral drugs include inter alia a nucleoside or nucleotide analog such as ADV, LMV, FCV, FTC, ETV, TDF, DAPD and DXG. For example, and without limiting the present invention to any one theory or mode of action, the location of individual residues and residue regions present on the HBV polymerase molecule has been analyzed in terms of their potential to function as part of the nucleotide binding pocket or alter the conformation of the nucleotide binding pocket. Based on this analysis, the HBV polymerase residues involved in determining the conformation of the binding pocket, or altering access to the nucleotide-binding pocket have been identified in accordance with the present invention. Mutations at these residues have the potential to alter which nucleotides or nucleoside analogs can bind to the nucleotide binding pocket of HBV polymerase. These residues are defined by reference to a numerical identification of amino acid residues or an amino acid residue region corresponding to the numbered residues as detailed in SEQ ID NO:1 or an amino acid sequence defining an HBV polymerase having at least 70% similarity to SEQ ID NO:1. Single residues are indicated by a single number and contiguous peptide regions as numerical ranges.

One or more of the following amino acids or amino acid regions are proposed to be involved in the binding of nucleotide and nucleoside analogs within a region selected from amino acid residues 28-36, 39-45, 59-66, 69-70, 73-93, 167-184, 198-213, 230-241 and 245-257 or 4-10, 24-27, 46-58, 67-68, 71-72, 94-120, 165-166, 185-197, 214-227, 242-244 and 258-266 as well as rtA21, rtA38, rtY54, rtN76, rtL91, rtF122, rtY124, rtT128, rtQ130, rtT184, rtM204, rtS202, rtH248, rtY252, rtS21, rtN/S/T/I/V53, rtY54, rtS57, rtL91, rtS116, rtL122, rtF122, rtN124, rtY124 rtH126, rtY126, rtT128N, rtP130, rtD131, rtV134, rtY135, rtY141, rtL145, rtF151, rtL180, rtA181, rtS202, rtI204, rtK212, rtL217, rtS219, rtI235, rtN236, rtN238, sP120, sM125, sS126, sT127, sT118, sM133, sM133, sF134, sS143, sD144, sG145, sW172, sI195, sS207, sY225, spacerL97, spacerK115, spacerH116, spacerL128, spacerS137, spacerR139, spacerF142, rtA97, rtH126, rtS135, rtM204, PreS1 N114, PreS1 T115, PreS2 F22, PreS2 V39, PreS2 P52, sL89, sT118, sF161, sE164, sI195, sI208, PreS1 E86, PreS1 N91, PreS2 P41, sQ30, sP120, sL176, sV194, rtS21, rtL122, rtN124, rtH126, rtP130, rtD131, rtY135, rtN/S/T/I/V53, rtY126, rtS202, rtI204, rtI235, sM125, sT127, sT118, sM133, sF134, sI195, sS207, sY225, rtG172, rtG174, rtP177, rtL180, rtT184, sR160, sE164, sF170, sL175, sQ181, sC/W182, sW196, sW196, sW196, sM198, sW199, sS204, sY206, sS210, sS210, sL216, sY255, rtL77, rtL77, rtL80, rtL80, rtH90, rtS117, rt125, rt128, rtQ125, rtQ125, rtY126Q, rtL128, rtT128, rtL132, rtN134, rtS137, rtN139, rtN139, rtY141, rtV/G142, rtL147, rtK149, rtG153, rtR153, rtW153, rtW153, rtF166, rtI169, rtF178, rtI187, rtI187, rtV191, rtV191, rtN202, rtS202, rtS202, rtS213, rtV/G214, rtS219, rtS219, rtN/Q238, rtN/S/H238, rtN/S/H/T238, rtR242, rtR242, rtN248, rtI253, s118-207, s117-120, sI68, sC69, sL109, sG112, sS17, sT118, sK122, sT123, sT126, sT131, sN131, sM133, sM133, sY/F134, sC139, sK141, sD144, sG145, rtT128, rtL82, rtT135, rtT150, rtV163, rtT184, rtA200, rtF202, rtS213, rtQ215, rtS219, rtA222, rtI224, rtL229, rtL235, rtN238, rtS78, rt116DEL122, rtI163, rtL180, rtE8, rtV23, rtD31, rtY53, rtV58, rtA/S21, rtV/I/N/S/T53, rtV/I/N/S/T53, rtS/T/N/H/A54, PreS2 L11, PreS2 R17, DEL PreS2 18-21, PreS2 T30, PreS2 N54, sT13, PreS2 Q1, PreS2 Q1, rtH90, rtL/F108, rtL157, rtA181, rtV207, rtP109, rtN/H/A/S/Q238, s181, sP214, sF83, sL173, sW199, sI126, sK160, sS174, sA84, sS210, sC69, sC76, s110, sY134 or sW172.

Another aspect of the present invention provides a computer-assisted method for identifying agents potentially able to bind to a domain of HBV polymerase and optionally modulate at least one functional activity of the HBV polymerase including predicting an anti-viral response to an agent using a programmed computer comprising the steps of:

-   (a) inputting into the progammed computer data comprising the atomic     co-ordinates of an HBV polymerase having a mutation selected from     within a region selected from amino acid residues 28-36, 39-45,     59-66, 69-70, 73-93, 167-184, 198-213, 230-241 and 245-257 or 4-10,     24-27, 46-58, 67-68, 71-72, 94-120, 165-166, 185-197, 214-227,     242-244 and 258-266 such as but not limited to rtA21S, rtA38E,     rtY54H, rtN76D, rtL91I, rtF122L, rtY124H, rtT128N, rtQ130P, rtT184G,     rtM204V/I, rtS202I, rtH248N, rtY252L, rtS21A, rtN/S/T/I/V53D,     rtY54H, rtS57P, rtL91I, rtS116P, rtL122F, rtF122L, rtN124H, rtY124H,     rtH126R, rtY126Q, rtT128N, rtP130Q, rtD131N, rtV134D, rtY135C,     rtY141Y/F, rtL145M, rtF151T/F, rtL180M, rtA181T, rtS202G, rtI204V,     rtK212R, rtL217R, rtS219A, rtI235I/M, rtN236T, rtN238D, sP120T,     sM125T, sS126T, sT127A, sT118R, sM133L/M, sM133T, sF134V, sS143S/T,     sD144A, sG145A, sW172Stop, sI195M, sS207R, sY225Y/C, spacerL97I,     spacerK115R, spacerH116L, spacerL128F, spacerS137G, spacerR139G,     spacerF142S, rtA97V, rtH126R, rtS135Y, rtM204I, PreS1 N114D, PreS1     T115S, PreS2 F22L, PreS2 V39A, PreS2 P52L, sL89V, sT118A, sF161L,     sE164D, sI195M, sI208T, PreS1 E86Q, PreS1 N91K, PreS2 P41H, sQ30K,     sP120T, sL176V, sV194F, rtS21A, rtL122F, rtN124H, rtH126R, rtP130Q,     rtD131N, rtY135C, rtN/S/T/I/V53D, rtY126Q, rtS202G, rtI204V,     rtI235I/M, sM125T, sT127A, sT118R, sM133T, sF134V, sI195M, sS207R,     sY225Y/C, rtG172E, rtG174C, rtP177L, rtL180V, rtT184S, sR160N,     sE164D, sF170L, sL175L/S, sQ181E/G/Q, sC/W182Y/STOP, sW196L, sW196S,     sW196STOP, sM198I, sW199S, sS204T, sY206N, sS210K, sS210R,     sL216STOP, sY255F, rtL77L/F, rtL77L/M/V, rtL80I, rtL80V, rtH90N/H,     rtS117S/Y, rt125DELrt128, rtQ125K, rtQ125N, rtY126Q, rtL128L/M,     rtT128A, rtL132L/M, rtN134G, rtS137T, rtN139H, rtN139K,     rtY141Y/STOP, rtV/G142L, rtL147L/W, rtK149R, rtG153E, rtR153Q,     rtW153S, rtW153Q, rtF166L, rtI169L, rtF178F/L, rtI187L, rtI187I/V,     rtV191I, rtV191V/I, rtN202S, rtS202S/C, rtS202G, rtS213T, rtV/G214E,     rtS219A, rtS219P, rtN/Q238H, rtN/S/H238N/K, rtN/S/H/T238/T/A/S/L,     rtR242R/K, rtR242R/S, rtN248H, rtI253A, s118-207, s117-120DEL,     sI68I/M, sC69F/L, sL109I/L, sG112R, sS17T, sT118R, sK122R, sT123P,     sT126S, sT131N, sN131T, sM133K/M, sM133I, sY/F134S, sC139C/G,     sK141E, sD144E, sG145R, rtT128T/I, rtL82M, rtT135C, rtT150A,     rtV163I, rtT184S, rtA200V, rtF202V, rtS213T, rtQ215H, rtS219A,     rtA222T, rtI224S, rtL229M, rtL235I, rtN238S, rtS78T, rt116DEL122,     rtI163V, rtL180V, rtE8A, rtV23I, rtD31D/G, rtY53D, rtV58V/I,     rtA/S21T, rtV/I/N/S/T53D, rtV/I/N/S/T53Y, rtS/T/N/H/A54Y/H, PreS2     L11L/A, PreS2 R171, DEL PreS2 18-21, PreS2 T30A, PreS2 N54H,     sT13T/A, PreS2 Q1V, PreS2 Q1M, rtH90D, rtL/F108L, rtL157L/M,     rtA181V, rtV207I, rtP109S, rtN/H/A/S/Q238K, s181M, sP214Q, sF83S,     sL173F, sW199L, sI126T, sK160R, sS174N, sA84V, sS210N, sC69STOP/C,     sC76Y, si110V/I, sY134N, sW172STOP/W,     K32M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     N33D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     P34S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     H35I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     T37W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P59S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     K60M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     F61P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     A62R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     V63A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     D83C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/deletion;     V84A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     S85T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     A86R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/YV/deletion;     Y89V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     H901/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     I/L91K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/deletion;     P177S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     F178P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     L179K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     L180K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     A181R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     Q183E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     F183P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     T184W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     Y203V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     M204F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     L235K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N236D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     T237W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P237S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     N238D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H238I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     A238R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     S239T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     Q238E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     K239M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     L247K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N248D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H248I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     F249P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     M250F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     G251H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/deletion; and     V251A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; -   (b) generating, using computer methods, a set of atomic co-ordinates     of a structure that possesses stereochemical complementarity to the     atomic co-ordinates defined in (a) or a subset thereof, thereby     generating a criteria data set; -   (c) comprising, using the processor, the criteria data set to a     computer database of chemical structures; -   (d) selecting from the database, using computer methods, chemical     structures which are similar to a portion of said criteria data set;     and -   (e) outputting the selected chemical structures which are similar to     a portion of the criteria data set.

Preferably, the method further comprises the step of obtaining an agent with a chemical structure selected in steps (d) and (e) and testing the compound for the ability to modulate at least one functional activity of an HBV polymerase.

Yet another aspect of the present invention provides a computer or a software component thereof for producing a three-dimensional representation of a molecule or molecular complex, which comprises a three-dimensional representation of a homolog of the molecule or molecular complex, which comprises a three-dimensional representation of a homolog of the molecule or molecular complex, in which the homolog comprises a domain that has a root mean square deviation from the backbone atoms of the amino acids of not more than 1.5 Å, in which the computer comprises:

-   (a) a machine-readable data storage medium comprising a data storage     material encoded with machine-readable data, wherein the data     comprises the structure co-ordinates of an HBV polymerase having a     mutation selected from within a region selected from amino acid     residues 28-36, 39-45, 59-66, 69-70, 73-93, 167-184, 198-213,     230-241 and 245-257 or 4-10, 24-27, 46-58, 67-68, 71-72, 94-120,     165-166, 185-197, 214-227, 242-244 and 258-266 such as but not     limited to rtA21S, rtA38E, rtY54H, rtN76D, rtL91I, rtF122L, rtY124H,     rtT128N, rtQ130P, rtT184G, rtM204V/I, rtS202I, rtH248N, rtY252L,     rtS21A, rtN/S/T/I/V53D, rtY54H, rtS57P, rtL91I, rtS116P, rtL122F,     rtF122L, rtN124H, rtY124H, rtH126R, rtY126Q, rtT128N, rtP130Q,     rtD131N, rtV134D, rtY135C, rtY141Y/F, rtL145M, rtF151T/F, rtL180M,     rtA181T, rtS202G, rtI204V, rtK212R, rtL217R, rtS219A, rtI235I/M,     rtN236T, rtN238D, sP120T, sM125T, sS126T, sT127A, sT118R, sM133L/M,     sM133T, sF134V, sS143S/T, sD144A, sG145A, sW172Stop, sI195M, sS207R,     sY225Y/C, spacerL97I, spacerK115R, spacerH116L, spacerL128F,     spacerS137G, spacerR139G, spacerF142S, rtA97V, rtH126R, rtS135Y,     rtM204I, PreS1 N114D, PreS1 T115S, PreS2 F22L, PreS2 V39A, PreS2     P52L, sL89V, sT118A, sF161L, sE164D, sI195M, sI208T, PreS1 E86Q,     PreS1 N91K, PreS2 P41H, sQ30K, sP120T, sL176V, sV194F, rtS21A,     rtL122F, rtN124H, rtH126R, rtP130Q, rtD131N, rtY135C,     rtN/S/T/I/V53D, rtY126Q, rtS202G, rtI204V, rtI235I/M, sM125T,     sT127A, sT118R, sM133T, sF134V, sI195M, sS207R, sY225Y/C, rtG172E,     rtG174C, rtP177L, rtL180V, rtT184S, sR160N, sE164D, sF170L,     sL175L/S, sQ181E/G/Q, sC/W182Y/STOP, sW196L, sW196S, sW196STOP,     sM198I, sW199S, sS204T, sY206N, sS210K, sS210R, sL216STOP, sY255F,     rtL77L/F, rtL77L/M/V, rtL80I, rtL80V, rtH90N/H, rtS117S/Y,     rt125DELrt128, rtQ125K, rtQ125N, rtY126Q, rtL128L/M, rtT128A,     rtL132L/M, rtN134G, rtS137T, rtN139H, rtN139K, rtY141Y/STOP,     rtV/G142L, rtL147L/W, rtK149R, rtG153E, rtR153Q, rtW153S, rtW153Q,     rtF166L, rtI169L, rtF178F/L, rtI187L, rtI187I/V, rtV191I, rtV191V/I,     rtN202S, rtS202S/C, rtS202G, rtS213T, rtV/G214E, rtS219A, rtS219P,     rtN/Q238H, rtN/S/H238N/K, rtN/S/H/T238/T/A/S/L, rtR242R/K,     rtR242R/S, rtN248H, rtI253A, s118-207, s117-120DEL, sI68I/M,     sC69F/L, sL109I/L, sG112R, sS17T, sT118R, sK122R, sT123P, sT126S,     sT131N, sN131T, sM133K/M, sM133I, sY/F134S, sC139C/G, sK141E,     sD144E, sG145R, rtT128T/I, rtL82M, rtT135C, rtT150A, rtV163I,     rtT184S, rtA200V, rtF202V, rtS213T, rtQ215H, rtS219A, rtA222T,     rtI224S, rtL229M, rtL235I, rtN238S, rtS78T, rt116DEL122, rtI163V,     rtL180V, rtE8A, rtV23I, rtD31D/G, rtY53D, rtV58V/I, rtA/S21T,     rtV/I/N/S/T53D, rtV/I/N/S/T53Y, rtS/T/N/H/A54Y/H, PreS2 L11L/A,     PreS2 R171, DEL PreS2 18-21, PreS2 T30A, PreS2 N54H, sT13T/A, PreS2     Q1V, PreS2 Q1M, rtH90D, rtL/F108L, rtL157L/M, rtA181V, rtV207I,     rtP109S, rtN/H/A/S/Q238K, s181M, sP214Q, sF83S, sL173F, sW199L,     sI126T, sK160R, sS174N, sA84V, sS210N, sC69STOP/C, sC76Y, si110V/I,     sY134N, sW172STOP/W,     K32M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     N33D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     P34S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     H35I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     T37W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P59S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     K60M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     F61P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     A62R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     V63A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     D83C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/deletion;     V84A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     S85T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     A86R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/YV/deletion;     Y89V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     H901/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     I/L91K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/deletion;     P177S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     F178P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     L179K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     L180K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     A181R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     Q183E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     F183P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     T184W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     Y203V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     M204F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     L235K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N236D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     T237W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P237S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     N238D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H238I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     A238R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     S239T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     Q238E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     K239M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     L247K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N248D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H248I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     F249P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     M250F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     G251H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/deletion; and     V251A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; -   (b) a working memory for storing instructions for processing the     machine-readable data; -   (c) a central-processing unit coupled to the working memory and to     the machine-readable data storage medium for processing the     machine-readable data into the three-dimensional representation; and -   (d) a display coupled to the central-processing unit for displaying     the three-dimensional representation.

In one embodiment, the three-dimensional representation is of an HBV polymerase defined by the set of structure co-ordinates set out in Table 6 or wherein the three-dimensional representation is of a homolog of the molecule or molecular complex, the homolog having a root mean square deviation from the backbone atoms of the amino acids of not more than 1.5 Å.

An additional aspect of the present invention provides a computer or a software component thereof for determining at least a portion of the structure co-ordinates corresponding to a three-dimensional structure of a molecule or molecular complex comprising an HBV polymerase in which the computer comprises:

-   (a) a machine-readable data storage medium comprising a data storage     material encoded with machine-readable data, in which the data     comprises at least a portion of the structural co-ordinates of an     HBV polymerase having a mutation selected from within a region     selected from amino acid residues 28-36, 39-45, 59-66, 69-70, 73-93,     167-184, 198-213, 230-241 and 245-257 or 4-10, 24-27, 46-58, 67-68,     71-72, 94-120, 165-166, 185-197, 214-227, 242-244 and 258-266 such     as but not limited to rtA21S, rtA38E, rtY54H, rtN76D, rtL91I,     rtF122L, rtY124H, rtT128N, rtQ130P, rtT184G, rtM204V/I, rtS202I,     rtH248N, rtY252L, rtS21A, rtN/S/T/I/V53D, rtY54H, rtS57P, rtL91I,     rtS116P, rtL122F, rtF122L, rtN124H, rtY124H, rtH126R, rtY126Q,     rtT128N, rtP130Q, rtD131N, rtV134D, rtY135C, rtY141Y/F, rtL145M,     rtF151T/F, rtL180M, rtA181T, rtS202G, rtI204V, rtK212R, rtL217R,     rtS219A, rtI235I/M, rtN236T, rtN238D, sP120T, sM125T, sS126T,     sT127A, sT118R, sM133L/M, sM133T, sF134V, sS143S/T, sD144A, sG145A,     sW172Stop, sI195M, sS207R, sY225Y/C, spacerL97I, spacerK115R,     spacerH116L, spacerL128F, spacerS137G, spacerR139G, spacerF142S,     rtA97V, rtH126R, rtS135Y, rtM204I, PreS1 N114D, PreS1 T115S, PreS2     F22L, PreS2 V39A, PreS2 P52L, sL89V, sT118A, sF161L, sE164D, sI195M,     sI208T, PreS1 E86Q, PreS1 N91K, PreS2 P41H, sQ30K, sP120T, sL176V,     sV194F, rtS21A, rtL122F, rtN124H, rtH126R, rtP130Q, rtD131N,     rtY135C, rtN/S/T/I/V53D, rtY126Q, rtS202G, rtI204V, rtI235I/M,     sM125T, sT127A, sT118R, sM133T, sF134V, sI195M, sS207R, sY225Y/C,     rtG172E, rtG174C, rtP177L, rtL180V, rtT184S, sR160N, sE164D, sF170L,     sL175L/S, sQ181E/G/Q, sC/W182Y/STOP, sW196L, sW196S, sW196STOP,     sM198I, sW199S, sS204T, sY206N, sS210K, sS210R, sL216STOP, sY255F,     rtL77L/F, rtL77L/M/V, rtL80I, rtL80V, rtH90N/H, rtS117S/Y,     rt125DELrt128, rtQ125K, rtQ125N, rtY126Q, rtL128L/M, rtT128A,     rtL132L/M, rtN134G, rtS137T, rtN139H, rtN139K, rtY141Y/STOP,     rtV/G142L, rtL147L/W, rtK149R, rtG153E, rtR153Q, rtW153S, rtW153Q,     rtF166L, rtI169L, rtF178F/L, rtI187L, rtI187I/V, rtV191I, rtV191V/I,     rtN202S, rtS202S/C, rtS202G, rtS213T, rtV/G214E, rtS219A, rtS219P,     rtN/Q238H, rtN/S/H238N/K, rtN/S/H/T238/T/A/S/L, rtR242R/K,     rtR242R/S, rtN248H, rtI253A, s118-207, s117-120DEL, sI68I/M,     sC69F/L, sL109I/L, sG112R, sS17T, sT118R, sK122R, sT123P, sT126S,     sT131N, sN131T, sM133K/M, sM133I, sY/F134S, sC139C/G, sK141E,     sD144E, sG145R, rtT128T/I, rtL82M, rtT135C, rtT150A, rtV163I,     rtT184S, rtA200V, rtF202V, rtS213T, rtQ215H, rtS219A, rtA222T,     rtI224S, rtL229M, rtL235I, rtN238S, rtS78T, rt116DEL122, rtI163V,     rtL180V, rtE8A, rtV23I, rtD31D/G, rtY53D, rtV58V/1, rtA/S21T,     rtV/I/N/S/T53D, rtV/I/N/S/T53Y, rtS/T/N/H/A54Y/H, PreS2 L11L/A,     PreS2 R171, DEL PreS2 18-21, PreS2 T30A, PreS2 N54H, sT13T/A, PreS2     Q1V, PreS2 Q1M, rtH90D, rtL/F108L, rtL157L/M, rtA181V, rtV207I,     rtP109S, rtN/H/A/S/Q238K, s181M, sP214Q, sF83S, sL173F, sW199L,     sI126T, sK160R, sS174N, sA84V, sS210N, sC69STOP/C, sC76Y, si110V/I,     sY134N, sW172STOP/W,     K32M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     N33D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     P34S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     H35I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     T37W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P59S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     K60M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     F61P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     A62R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     V63A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     D83C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/deletion;     V84A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     S85T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     A86R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/YV/deletion;     Y89V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     H90I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     I/L91K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/deletion;     P177S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     F178P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     L179K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     L180K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     A181R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     Q183E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     F183P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     T184W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     Y203V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     M204F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     L235K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N236D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     T237W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P237S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     N238D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H238I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     A238R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     S239T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     Q238E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     K239M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     L247K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N248D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H248I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     F249P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     M250F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     G251H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/deletion; and     V251A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; -   (b) a machine-readable data storage medium comprising a data storage     material encoded with machine-readable data, wherein the data     comprises atomic co-ordinates of the molecule or molecular complex; -   (c) a working memory for storing instructions for processing the     machine-readable data of (a) and (b); -   (d) a central-processing unit coupled to the working memory and to     the machine-readable data storage medium of (a) and (b) for     performing a transformation of the machine readable data of (a) and     for processing the machine-readable data of (b) into structure     co-ordinates; and -   (e) a display coupled to the central-processing unit for displaying     the structure co-ordinates of the molecule or molecular complex.

More particularly, the computer product is based on amino acid resides involved in binding of nucleoside or nucleotide analogs. Accordingly, the present invention provides a computer-assisted method for identifying agents potentially able to bind to a domain of HBV polymerase and optionally modulate at least one functional activity of the HBV polymerase including predicting an anti-viral response to an agent using a programmed computer comprising the steps of:

-   (a) inputting into the progammed computer data comprising the atomic     co-ordinates of an HBV polymerase or fragment thereof at positions     28-36, 39-45, 59-66, 69-70, 73-93, 167-184, 198-213, 230-241 and     245-257 and/or at position numbers 4-10, 24-27, 46-58, 67-68, 71-72,     94-120, 165-166, 185-197, 214-227, 242-244 and 258-266; -   (b) generating, using computer methods, a set of atomic co-ordinates     of a structure that possesses stereochemical complementarity to the     atomic co-ordinates defined in (a) or a subset thereof, thereby     generating a criteria data set; -   (c) comprising, using the processor, the criteria data set to a     computer database of chemical structures; -   (d) selecting from the database, using computer methods, chemical     structures which are similar to a portion f said criteria data set;     and -   (e) outputting the selected chemical structures which are similar to     a portion of the criteria data set.

The binding of ADV to HBV polymerase has been particularly investigated in accordance with the present invention. This interaction is schematically depicted in FIG. 6. Based on this analysis, the HBV polymerase molecule binding regions and specific residues which are thought to be involved in ADV binding have been identified. HBV polymerases with substitutions at particular amino acid residues (when compared to native HBV polymerase) which exhibit resistance to ADV have also been identified. The specific amino acid substitutions which are involved in the binding of ADV to HBV polymerase which are reflected in the anti-viral drug-resistant HBV polymerase amino acid sequence provided in SEQ ID NO:1 have also been identified. These are detailed as substitutions with reference to native HBV polymerase: rtN236T, rtA181T, rtA181V, rtV84N and rtH90D.

However, to the extent that any other HBV polymerase is utilized for the purpose of the method defined herein, the precise residue numbers of the location of these regions may vary. The present invention should be understood to encompass equivalent regions and residues which are present on forms of the HBV polymerase molecule other than that identified by SEQ ID NO:1. In particular, HBV polymerases resistant to ADV, LMV, FCV, FTC, ETV, TDF, DAPD and DXG are also contemplated by the present invention. Such polymerases are encompassed by reference to an amino acid sequence having at least about 70% similarity to SEQ ID NO:1 after optimal alignment.

The determination of these potential binding regions has been made possible by the elucidation of the three dimensional structure of the HBV polymerase which facilitates the identification and/or rational modification and design of agents which can be used to bind to the nucleotide binding pocket of anti-viral drug-resistant HBV polymerase according to the present invention.

Accordingly, another embodiment of the present invention provides a method for identifying an agent capable of interacting with an anti-viral drug-resistant HBV polymerase, said method comprising contacting an anti-viral drug-resistant HBV polymerase or derivative, homolog, analog, fragment or equivalent thereof, which molecule comprises the amino acid sequence set forth in SEQ ID NO:1 or an amino acid sequence having at least 70% similarity to SEQ ID NO:1 after optimal alignment with an agent and assessing the degree of interactive complementarity of said agent with said HBV polymerase wherein said agent binds to the nucleotide binding pocket of said HBV polymerase.

The agents may modulate at least one functional activity associated with the HBV polymerase. Alternatively or in addition, the interactions alone is sufficient for the agent to be useful as a therapeutic agent.

The term “modulate” should be understood to refer to the up-regulation or down-regulation of at least one functional activity associated with the HBV polymerase. Down-regulation of the HBV polymerase associated functional activity, for example, inhibiting replication of the HBV, is particularly desirable in the treatment of diseases such as hepatitis. Accordingly, the present invention provides a potential therapeutic or prophylactic treatment for hepatitis which is unresponsive to ADV or another anti-viral agent such as a nucleoside or nucleotide analog.

Accordingly, the present invention is directed to a method for identifying an agent capable of interacting with an anti-viral drug-resistant HBV polymerase and/or a wild-type HBV polymerase and optionally down-regulating at least one functional activity associated with said HBV polymerase wherein said anti-viral resistant HBV polymerase and/or wild-type HBV polymerase has at least one of the following characteristics:

-   (i) displays increased resistance or decreased sensitivity to a     nucleoside analog such as ADV, LMV, FCV, FTC, ETV, TDF, DAPD and DXG     compared to native HBV polymerase; -   (ii) comprises a mutation selected from within a region selected     from amino acid residues 28-36, 39-45, 59-66, 69-70, 73-93, 167-184,     198-213, 230-241 and 245-257 or 4-10, 24-27, 46-58, 67-68, 71-72,     94-120, 165-166, 185-197, 214-227, 242-244 and 258-266 such as but     not limited to rtA21S, rtA38E, rtY54H, rtN76D, rtL91I, rtF122L,     rtY124H, rtT128N, rtQ130P, rtT184G, rtM204V/I, rtS202I, rtH248N,     rtY252L, rtS21A, rtN/S/T/I/V53D, rtY54H, rtS57P, rtL91I, rtS116P,     rtL122F, rtF122L, rtN124H, rtY124H, rtH126R, rtY126Q, rtT128N,     rtP130Q, rtD131N, rtV134D, rtY135C, rtY141Y/F, rtL145M, rtF151T/F,     rtL180M, rtA181T, rtS202G, rtI204V, rtK212R, rtL217R, rtS219A,     rtI235I/M, rtN236T, rtN238D, sP120T, sM125T, sS126T, sT127A, sT118R,     sM133L/M, sM133T, sF134V, sS143S/T, sD144A, sG145A, sW172Stop,     sI195M, sS207R, sY225Y/C, spacerL97I, spacerK115R, spacerH116L,     spacerL128F, spacerS137G, spacerR139G, spacerF142S, rtA97V, rtH126R,     rtS135Y, rtM204I, PreS1 N114D, PreS1 T115S, PreS2 F22L, PreS2 V39A,     PreS2 P52L, sL89V, sT118A, sF161L, sE164D, sI195M, sI208T, PreS1     E86Q, PreS1 N91K, PreS2 P41H, sQ30K, sP120T, sL176V, sV194F, rtS21A,     rtL122F, rtN124H, rtH126R, rtP130Q, rtD131N, rtY135C,     rtN/S/T/I/V53D, rtY126Q, rtS202G, rtI204V, rtI235I/M, sM125T,     sT127A, sT118R, sM133T, sF134V, sI195M, sS207R, sY225Y/C, rtG172E,     rtG174C, rtP177L, rtL180V, rtT184S, sR160N, sE164D, sF170L,     sL175L/S, sQ181E/G/Q, sC/W182Y/STOP, sW196L, sW196S, sW196STOP,     sM198I, sW199S, sS204T, sY206N, sS210K, sS210R, sL216STOP, sY255F,     rtL77L/F, rtL77L/M/V, rtL80I, rtL80V, rtH90N/H, rtS117S/Y,     rt125DELrt128, rtQ125K, rtQ125N, rtY126Q, rtL128L/M, rtT128A,     rtL132L/M, rtN134G, rtS137T, rtN139H, rtN139K, rtY141Y/STOP,     rtV/G142L, rtL147L/W, rtK149R, rtG153E, rtR153Q, rtW153S, rtW153Q,     rtF166L, rtI169L, rtF178F/L, rtI187L, rtI187I/V, rtV191I, rtV191V/I,     rtN202S, rtS202S/C, rtS202G, rtS213T, rtV/G214E, rtS219A, rtS219P,     rtN/Q238H, rtN/S/H238N/K, rtN/S/H/T238/T/A/S/L, rtR242R/K,     rtR242R/S, rtN248H, rtI253A, s118-207, s117-120DEL, sI68I/M,     sC69F/L, sL109I/L, sG112R, sS17T, sT118R, sK122R, sT123P, sT126S,     sT131N, sN131T, sM133K/M, sM133I, sY/F134S, sC139C/G, sK141E,     sD144E, sG145R, rtT128T/I, rtL82M, rtT135C, rtT150A, rtV163I,     rtT184S, rtA200V, rtF202V, rtS213T, rtQ215H, rtS219A, rtA222T,     rtI224S, rtL229M, rtL235I, rtN238S, rtS78T, rt116DEL122, rtI163V,     rtL180V, rtE8A, rtV23I, rtD31D/G, rtY53D, rtV58V/I, rtA/S21T,     rtV/I/N/S/T53D, rtV/I/N/S/T53Y, rtS/T/N/H/A54Y/H, PreS2 L11L/A,     PreS2 R171, DEL PreS2 18-21, PreS2 T30A, PreS2 N54H, sT13T/A, PreS2     Q1V, PreS2 Q1M, rtH90D, rtL/F108L, rtL157L/M, rtA181V, rtV207I,     rtP109S, rtN/H/A/S/Q238K, s181M, sP214Q, sF83S, sL173F, sW199L,     sI126T, sK160R, sS174N, sA84V, sS210N, sC69STOP/C, sC76Y, si110V/I,     sY134N, sW172STOP/W,     K32M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     N33D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     P34S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     H35I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     T37W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P59S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     K60M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     F61P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     A62R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     V63A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     D83C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/deletion;     V84A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     S85T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     A86R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/YV/deletion;     Y89V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     H901/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     I/L91K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/deletion;     P177S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     F178P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     L179K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     L180K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     A181R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     Q183E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     F183P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     T184W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     Y203V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     M204F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     L235K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N236D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     T237W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P237S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     N238D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H238I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     A238R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     S239T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     Q238E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     K239M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     L247K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N248D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H248I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     F249P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     M250F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     G251H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/deletion; and     V251A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; and/or -   (iii) comprises the amino acid sequence set forth in SEQ ID NO:1 or     an amino acid sequence defining an HBV polymerase and having a     sequence which is at least 70% similar after optimal alignment to     SEQ ID NO:1;     said method comprising contacting said anti-viral resistant HBV     polymerase molecule or derivative, homolog, analog, fragment, mutant     or equivalent thereof with an agent and assessing the degree of     interactive complementarity of said agent with said anti-viral     drug-resistant HBV polymerase.

Preferably, the functional activity of the HBV polymerase involves replication of HBV.

More preferably, insofar as the HBV polymerase is resistant to or has reduced sensitivity to ADV, the HBV polymerase has the atomic co-ordinates substantially as set forth in Table 6.

Alternatively, the agent interacts with but does not inhibit the HBV polymerase. Such agents have potential as diagnostic agents, such as being able to discriminate between HBV polymerases of different strains.

It should be understood that modulation of “at least one functional activity” associated with the HBV polymerase is intended as a reference to the modulation of the functional activities which are associated with the replication of the HBV. “Associated” is meant that the subject functional activity is either directly or indirectly regulated by the level of HBV polymerase molecule activation or deactivation. Directly associated functional activity includes, but is not limited to, duplication of the HBV genome by de novo synthesis of a new nucleic acid strand from a template nucleic acid.

Reference to an “agent” should be understood as a reference to any proteinaceous or non-proteinaceous molecule which achieves the object of the present invention, i.e. the modulation of at least one functional activity associated with the HBV polymerase molecule.

The proteinaceous molecule may be derived from natural or recombinant sources including fusion proteins or following, for example, natural product screening. The non-proteinaceous molecule may be, for example, a synthetic molecule, such as one which is chemically synthesized, or it may be derived from natural sources, such as, for example, obtained through natural product screening. The present invention contemplates chemical analogs of the nucleotide bases or small molecules capable of acting as agonists or antagonists of the HBV polymerase. Chemical agonists may not necessarily be derived from HBV polymerase molecule ligands but may share certain conformational similarities.

Alternatively, chemical agonists may be specifically designed to mimic certain physicochemical properties. Antagonists may be any compound capable of blocking, inhibiting or otherwise preventing the HBV polymerase from carrying out its normal biological functions. Antagonists and agonists include inter alia monoclonal antibodies, small molecules, peptides or drugs.

Without limiting the application of the present invention in any way, the method of the present invention facilitates the identification, analysis, design and/or modification of agents capable of interacting with an anti-viral drug-resistant HBV polymerase molecule. In this regard, such agents may be identified by:

-   -   (i) Randomly screening (for example, utilizing routine         high-throughput screening technology) to identify agents which         exhibit some modulatory capacity with respect to HBV polymerase         functional activity and analyzing the precise nature and         magnitude of the agent's signaling capacity utilizing the method         of the present invention. In this regard, existing crystals may         be soaked with the agents or co-crystallization may be         performed. A combination of modeling and synthetic modification         of the local compound together with mutagenesis of the HBV         polymerase may then be performed. In screening for agents which         may modulate activity, standard methods of phage display and         also combinatorial chemistry may be utilized (Goodson et al.,         Proc. Natl. Acad. Sci. USA 91(15): 7129-7133, 1994; Terrett,         Drug Discov. Today 5(5): 211-212, 2000). Such interaction         studies can also be furthered utilizing techniques such as the         Biacore analysis and NMR perturbation studies detailed earlier.         Such agents are often commonly referred to as “lead” agents in         terms of the random screening of proteinaceous or         non-proteinaceous molecules for their capacity to function         either agonistically or antagonistically. Further, for example,         binding affinity and specificity could be enhanced by modifying         lead agents to maximize interactions with nearby residues of βc         revealed from the structure of the complex. Such analyzes would         facilitate the selection of agents which are the most suitable         for a given purpose. In this way, the selection step is based         not only on in vitro data but also on a technical analysis of         sites of agent: HBV polymerase molecule interactions in terms of         their frequency, stability and suitability for a given purpose.         For example, analysis performed in accordance with the method of         the present invention may reveal that what appears to be an         acceptable in vitro activity in respect of a randomly identified         agent is in fact induced by a highly unstable interaction due to         the presence of proximally located agent: HBV polymerase         molecule sites which exhibit significant repulsive forces         thereby destabilizing the overall interaction between the agent         and the HBV polymerase molecule. This would then facilitate the         selection of another prospective lead compound, exhibiting an         equivalent degree of in vitro activity, but which agent does         not, upon further analysis, involve the existence of such         destabilizing repulsive forces.     -   Screening for the modulatory agents herein defined can be         achieved by any one of several suitable methods which would be         well known to those of skill in the art and which are, for         example, routinely used to randomly screen proteinaceous and         non-proteinaceous molecules for the purpose of identifying lead         compounds. For example, such techniques would include contacting         a cell infected with HBV expressing the anti-viral resistant HBV         and screening for the modulation of HBV polymerase functional         activity or for HBV polymerase induced down-stream functional         activity including modulation of the replication of the virus.         Detecting such modulation can be achieved utilizing techniques         such as Western Blotting, electrophoretic mobility shift assays         and/or the titre of the virus in cell culture or animal models.         The choice of detection technique will depend entirely on the         nature of the HBV polymerase feature which is the subject of         detection.     -   It should be understood that the HBV polymerase molecule or         functional equivalent or derivative thereof may be         transgenically expressed in the cell which is the subject of         testing in the absence of viral infection or it may be as a         result of HBV infection of said cell. Further, the gene may be         constitutively expressed or may require stimulation in order to         effect expression. Further, the HBV polymerase may comprise the         entire HBV polymerase molecule gene or it may merely comprise a         portion of the gene such as the portion which codes for some of         the HBV polymerase domains.     -   These methods provide a mechanism for performing high throughput         screening of putative modulatory agents such as the         proteinaceous or non-proteinaceous agents comprising synthetic,         recombinant, chemical and natural libraries.     -   (ii) The candidate or lead agent (for example, the agent         identified in accordance with the methodology described in         relation to point (i)) could be modified in order to maximize         desired interactions (for example, binding affinity to         specificity) with the anti-viral resistant HBV polymerase         molecule and to minimize undesirable interactions (such as         repulsive or otherwise destabilizing interactions). Such         modification is only possible in light of a detailed knowledge         of the three-dimensional structure of the anti-viral resistant         HBV polymerase and the capacity therefore to identify regions of         functional importance, thereby facilitating the structural         modification of an agent to maximize an agonistic or         antagonistic interaction. Such methodology is particularly         applicable to rational drug design. Methods of modification of a         candidate or lead agent in accordance with the purpose as         defined herein would be well known to those of skill in the art.         For example, a molecular replacement program such as Amore         (Navaza, Acta Cryst. A50: 157-163, 1994) may be utilized in this         regard. The method of the present invention also facilitates the         mutagenesis of known signal inducing agents in order to ablate         or improve signaling activity.     -   (iii) In addition to analyzing fit and/or structurally modifying         existing molecules, the method of the present invention also         facilitates the rational design and synthesis of an agent, such         as an agonistic or antagonistic agent, based on theoretically         modeling an agent exhibiting the desired HBV polymerase molecule         interactive structural features followed by the synthesis and         testing of the subject agent.

It should be understood that any one or more of applications (i) to (iii) above may be utilized in identifying a particular agent.

As detailed earlier, reference to HBV polymerase includes reference to parts or fragments thereof since it may be useful to identify, analyze, design and/or modify agents which interact with only part of the HBV polymerase molecule structure. Accordingly, the method of the present invention should be understood to extend inter alia to the design of synthetic peptides to parts of the structure predicated to be important to the biological activity of the HBV polymerase or resistance of the HBV polymerase to anti-viral agents.

In this regard and in a particularly preferred embodiment, the method of the present invention is applied to the identification, analysis, design and/or modification of agents, such as nucleoside analogs, which bind to the nucleotide binding pocket of the anti-viral resistant HBV polymerase molecule.

In a related aspect, the present invention should be understood to encompass agents identified utilizing the methods herein defined.

Accordingly, the present invention is directed to an agent capable of interacting with an anti-viral resistant HBV polymerase molecule and/or a wild-type HBV polymerase and optionally modulating at least one functional activity associated with said polymerase wherein said anti-viral resistant HBV polymerase and/or wild-type HBV polymerase has at least one of the following characteristics:

-   (i) displays increased resistance or decreased sensitivity to a     nucleoside analog such as ADV, LMV, FCV, FTC, ETV, DAPD and DXG     compared to native HBV polymerase; -   (ii) comprises a mutation selected from within a region selected     from amino acid residues 28-36, 39-45, 59-66, 69-70, 73-93, 167-184,     198-213, 230-241 and 245-257 or 4-10, 24-27, 46-58, 67-68, 71-72,     94-120, 165-166, 185-197, 214-227, 242-244 and 258-266 such as but     not limited to rtA21S, rtA38E, rtY54H, rtN76D, rtL91I, rtF122L,     rtY124H, rtT128N, rtQ130P, rtT184G, rtM204V/I, rtS202I, rtH248N,     rtY252L, rtS21A, rtN/S/T/I/V53D, rtY54H, rtS57P, rtL91I, rtS116P,     rtL122F, rtF122L, rtN124H, rtY124H, rtH126R, rtY126Q, rtT128N,     rtP130Q, rtD131N, rtV134D, rtY135C, rtY141Y/F, rtL145M, rtF151T/F,     rtL180M, rtA181T, rtS202G, rtI204V, rtK212R, rtL217R, rtS219A,     rtI235I/M, rtN236T, rtN238D, sP120T, sM125T, sS126T, sT127A, sT118R,     sM133L/M, sM133T, sF134V, sS143S/T, sD144A, sG145A, sW172Stop,     sI195M, sS207R, sY225Y/C, spacerL97I, spacerK115R, spacerH116L,     spacerL128F, spacerS137G, spacerR139G, spacerF142S, rtA97V, rtH126R,     rtS135Y, rtM204I, PreS1 N114D, PreS1 T15, PreS2 F22L, PreS2 V39A,     PreS2 P52L, sL89V, sT118A, sF161L, sE164D, sI195M, sI208T, PreS1     E86Q, PreS1 N91K, PreS2 P41H, sQ30K, sP120T, sL176V, sV194F, rtS21A,     rtL122F, rtN124H, rtH126R, rtP130Q, rtD131N, rtY135C,     rtN/S/T/I/V53D, rtY126Q, rtS202G, rtI204V, rtI235I/M, sM125T,     sT127A, sT118R, sM133T, sF134V, sI195M, sS207R, sY225Y/C, rtG172E,     rtG174C, rtP177L, rtL180V, rtT184S, sR160N, sE164D, sF170L,     sL175L/S, sQ181E/G/Q, sC/W182Y/STOP, sW196L, sW196S, sW196STOP,     sM198I, sW199S, sS204T, sY206N, sS210K, sS210R, sL216STOP, sY255F,     rtL77L/F, rtL77L/M/V, rtL80I, rtL80V, rtH90N/H, rtS117S/Y,     rt125DELrt128, rtQ125K, rtQ125N, rtY126Q, rtL128L/M, rtT128A,     rtL132L/M, rtN134G, rtS137T, rtN139H, rtN139K, rtY141Y/STOP,     rtV/G142L, rtL147L/W, rtK149R, rtG153E, rtR153Q, rtW153S, rtW153Q,     rtF166L, rtI169L, rtF178F/L, rtI187L, rtI187I/V, rtV191I, rtV191V/I,     rtN202S, rtS202S/C, rtS202G, rtS213T, rtV/G214E, rtS219A, rtS219P,     rtN/Q238H, rtN/S/H238N/K, rtN/S/H/T238/T/A/S/L, rtR242R/K,     rtR242R/S, rtN248H, rtI253A, s118-207, s117-120DEL, sI68I/M,     sC69F/L, sL109I/L, sG112R, sS17T, sT118R, sK122R, sT123P, sT126S,     sT131N, sN131T, sM133K/M, sM133I, sY/F134S, sC139C/G, sK141E,     sD144E, sG145R, rtT128T/I, rtL82M, rtT135C, rtT150A, rtV163I,     rtT184S, rtA200V, rtF202V, rtS213T, rtQ215H, rtS219A, rtA222T,     rtI224S, rtL229M, rtL235I, rtN238S, rtS78T, rt116DEL122, rtI163V,     rtL180V, rtE8A, rtV23I, rtD31D/G, rtY53D, rtV58V/I, rtA/S21T,     rtV/I/N/S/T53D, rtV/I/N/S/T53Y, rtS/T/N/H/A54Y/H, PreS2 L11L/A,     PreS2 R171, DEL PreS2 18-21, PreS2 T30A, PreS2 N54H, sT13T/A, PreS2     Q1V, PreS2 Q1M, rtH90D, rtL/F108L, rtL157L/M, rtA181V, rtV207I,     rtP109S, rtN/H/A/S/Q238K, s181M, sP214Q, sF83S, sL173F, sW199L,     sI126T, sK160R, sS174N, sA84V, sS210N, sC69STOP/C, sC76Y, s110V/I,     sY134N, sW172STOP/W,     K32M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     N33D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     P34S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     H35I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     T37W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P59S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     K60M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     F61P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     A62R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     V63A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     D83C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/deletion;     V84A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion;     S85T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     A86R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/YV/deletion;     Y89V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     H90I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     I/L91K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/deletion;     P177S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     F178P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     L179K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     L180K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     A181R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     Q183E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     F183P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     T184W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     Y203V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion;     M204F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     L235K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N236D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     T237W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion;     P237S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion;     N238D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H238I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     A238R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion;     S239T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion;     Q238E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion;     K239M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion;     L247K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion;     N248D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion;     H248I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion;     F249P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion;     M250F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion;     G251H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/deletion; and     V251A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; and/or -   (iii) comprises the amino acid sequence set forth in SEQ ID NO:1 or     an amino acid sequence defining an HBV polymerase and having a     sequence which is at least 70% similar after optimal alignment to     SEQ ID NO:1;     wherein said agent is identified in accordance with the methods     hereinbefore defined.

Preferably, the agent can bind to the nucleotide binding pocket of the anti-viral resistant HBV polymerase.

Even more preferably, the anti-viral resistant HBV polymerase molecule is mapped to the atomic co-ordinates set forth in Table 6.

In another preferred embodiment, the functional activity of the HBV polymerase is associated with HBV replication.

In the context of this aspect of the present invention, the term “identified” includes an agent which has been analyzed, designed and/or modified in accordance with the methods herein defined.

A further aspect of the present invention relates to the use of agents identified utilizing the methods herein defined to modulate an HBV polymerase activity such as an anti-viral drug resistant HBV polymerase and in particular the use of these agents in the therapeutic and/or prophylactic treatment of conditions characterized by infection by an HBV. For example, antagonistic agents are particularly useful in anti-viral therapy in HBV infection in a subject wherein the HBV is resistant to an existing anti-viral agent, such as ADV, LMV, FCV, FTC, ETV, TDF, DAPD and DXG.

Accordingly, another aspect of the present invention provides a method modulating at least one functional activity associated with an anti-viral drug-resistant HBV polymerase in a subject, said method comprising introducing into said subject an effective amount of an agent, which agent is identified in accordance with the methods herein defined, for a time and under conditions sufficient for said agent to interact with said HBV polymerase molecule and to inhibit or reduce its activity.

In one embodiment, the agent inhibits HBV replication.

This aspect of the present invention encompasses both in vivo therapy as well as in vitro culture systems. The latter may be of benefit, for example, when screening for agents with antagonistic activity toward the anti-viral resistant HBV polymerase.

In yet another aspect, the present invention relates to a method for the treatment and/or prophylaxis of HBV infection, said method comprising administering to a subject an effective amount of an agent capable of modulating the activity of HBV polymerase of said virus, which agent is identified in accordance with the methods herein defined, for a time and under conditions sufficient for said agent to interact with said anti-viral resistant HBV polymerase molecule and inhibits its activity.

The molecule which may be administered to a subject in accordance with the present invention may also be linked to a targeting means such as a monoclonal antibody, which provides specific delivery of these molecules to the target cells.

In a preferred embodiment, the subject of the prophylactic or therapeutic treatment is a mammal and still more preferably a human.

Administration of the agent, in the form of a pharmaceutical composition, may be performed by any convenient means. The modulatory agent of the pharmaceutical composition is contemplated to exhibit therapeutic activity when administered in an amount which depends on the particular case. The variation depends, for example, on the human or animal and the modulatory agent chosen. A broad range of doses may be applicable. Considering a patient, for example, from about 0.01 μg to about 10 g of modulatory agent may be administered per kilogram of body weight per day. Dosage regimes may be adjusted to provide the optimum therapeutic response. For example, several divided doses may be administered daily, weekly, monthly or other suitable time intervals or the dose may be proportionally reduced as indicated by the exigencies of the situation. Exemplary amounts include 0.01, 0.02, 0.03, 0.04, 0.05, 0.06, 0.07, 0.08, 0.09 or 0.1 μg; 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 μg; 0.1, 0.2, 0.3, 0.4, 0.5, 0.6, 0.7, 0.8, 0.9 or 1 mg; 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 mg, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 or 100 mg; 100, 200, 300, 400, 500, 600, 700, 800, 900 or 1000 mg and 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 g. The agent may be administered in the form of pharmaceutically acceptable nontoxic salts, such as acid addition salts or metal complexes, e.g. with zinc, iron or the like (which are considered as salts for purposes of this application). Illustrative of such acid addition salts are hydrochloride, hydrobromide, sulphate, phosphate, maleate, acetate, citrate, benzoate, succinate, malate, ascorbate, tartrate and the like. If the active ingredient is to be administered in tablet form, the tablet may contain a binder such as tragacanth, corn starch or gelatin; a disintegrating agent, such as alginic acid; and a lubricant, such as magnesium stearate.

Routes of administration include, but are not limited to, respiratorally, intratracheally, nasopharyngeally, intravenously, intraperitoneally, subcutaneously, intracranially, intradermally, intramuscularly, intraoccularly, intrathecally, intracereberally, intranasally, infusion, orally, rectally, via IV drip patch and implant. Preferably, the route of administration is a route which permits directed delivery of the agent. For example, aerosol administration (such as by nebulization) into the airways permits directed delivery to the airways region, in contrast to systemic delivery which results in delivery to the whole body.

The formulation is administered in a therapeutically effective amount. A therapeutically effective amount means that amount necessary at least partly to attain the desired effect, or to delay the onset of, inhibit the progression of, or halt altogether, the onset or progression of the particular condition being treated. Such amounts will depend, of course, on the particular conditions being treated, the severity of the condition and individual subject parameters including age, physical conditions, size, weight and concurrent treatment. These factors are well known to those of ordinary skill in the art and can be addressed with no more than routine experimentation. It is preferred generally that a maximum dose be used, that is, the highest safe dose according to sound medical judgement. It will be understood by those of ordinary skill in the art, however, that a lower dose or tolerable dose may be administered for medical reasons, psychological reasons or for virtually any other reasons.

As indicated above, daily, weekly or monthly doses of formulation may be from about 0.01 μg/kg per day to 1000 mg/kg per day. Small doses (0.01-1 mg) may be administered initially, followed by increasing doses up to about 1000 mg/kg per day. In the event that the response in a subject is insufficient at such doses, even higher doses (or effective higher doses by a different, more localized delivery route) may be employed to the extent patient tolerance permits. A single dose may be administered or multiple doses may be required on an hourly, daily, weekly or monthly basis. Effective amounts of formulation vary depending on the individual but may range from about 0.1 μg to about 20 mg, alternatively from about 1 μg to about 10 mg and more preferably from about 1 μg to 5 mg per dose.

In another aspect the present invention relates to the use of an agent capable of modulating at least one functional activity associated with an anti-viral drug-resistant HBV polymerase, which agent is identified in accordance with the methods herein defined, in the manufacture of a medicament for the treatment and/or prophylaxis of HBV infection.

In another aspect, the present invention relates to the use of an agent, which agent is identified in accordance with the methods herein defined, in the manufacture of a medicament for the modulation of anti-viral drug-resistant HBV polymerase functional activity.

Yet another aspect relates to agents for use in modulating the functional activity of the anti-viral drug-resistant HBV polymerase molecule wherein said agent is identified in accordance with the methods herein defined.

Yet another aspect relates to agents for use in the treatment and/or prophylaxis of HBV infection wherein said agent is identified in accordance with the methods herein defined.

In a related aspect of the present invention the subject undergoing treatment may be a human or an animal in need of therapeutic or prophylactic treatment.

Reference herein to “treatment” and “prophylaxis” is to be considered in its broadest context. The term “treatment” does not necessarily imply that a mammal is treated until total recovery. Similarly, “prophylaxis” does not necessarily mean that the subject will not eventually contract a disease condition. Accordingly, treatment and prophylaxis include amelioration of the symptoms of a particular condition or preventing or otherwise reducing the risk of developing a particular condition. The term “prophylaxis” may be considered as reducing the severity of onset of a particular condition. “Treatment” may also reduce the severity of an existing condition or the frequency of acute attacks.

In accordance with these methods, the agent defined in accordance with the present invention may be co-administered with one or more other compounds or molecules. By “co-administered” is meant simultaneous administration in the same formulation or in two different formulations via the same or different routes or sequential administration by the same or different routes. By “sequential” administration is meant a time difference of from seconds, minutes, hours or days between the administration of the two types of molecules. These molecules may be administered in any order.

In yet another aspect, the present invention relates to a pharmaceutical composition comprising an agent as herein defined together with one or more pharmaceutically acceptable carriers and/or diluents.

The pharmaceutical forms of the subject compositions suitable for injectable use include sterile aqueous solutions (where water soluble) or dispersions and sterile powders for the extemporaneous preparation of sterile injectable solutions or dispersion or may be in the form of a cream or other form suitable for topical application. It must be stable under the conditions of manufacture and storage and must be preserved against the contaminating action of microorganisms such as bacteria and fungi. The carrier can be a solvent or dispersion medium containing, for example, water, ethanol, polyol (for example, glycerol, propylene glycol and liquid polyethylene glycol, and the like), suitable mixtures thereof, and vegetable oils. The proper fluidity can be maintained, for example, by the use of a coating such as lecithin, by the maintenance of the required particle size in the case of dispersion and by the use of superfactants. The preventions of the action of microorganisms can be brought about by various antibacterial and antifungal agents, for example, parabens, chlorobutanol, phenol, sorbic acid, thimerosal and the like. In many cases, it will be preferable to include isotonic agents, for example, sugars or sodium chloride. Prolonged absorption of the injectable compositions can be brought about by the use in the compositions of agents delaying absorption, for example, aluminum monostearate and gelatin.

Sterile injectable solutions are prepared by incorporating the active compounds in the required amount in the appropriate solvent with various of the other ingredients enumerated above, as required, followed by filtered sterilization. Generally, dispersions are prepared by incorporating the various sterilized active ingredient into a sterile vehicle which contains the basic dispersion medium and the required other ingredients from those enumerated above. In the case of sterile powders for the preparation of sterile injectable solutions, the preferred methods of preparation are vacuum drying and the freeze-drying technique which yield a powder of the active ingredient plus any additional desired ingredient from previously sterile-filtered solution thereof.

When the active ingredients are suitably protected they may be orally administered, for example, with an inert diluent or with an assimilable edible carrier, or it may be enclosed in hard or soft shell gelatin capsule, or it may be compressed into tablets, or it may be incorporated directly with the food of the diet. For oral therapeutic administration, the active compound may be incorporated with excipients and used in the form of ingestible tablets, buccal tablets, troches, capsules, elixirs, suspensions, syrups, wafers, and the like. Such compositions and preparations should contain at least 1% by weight of active compound. The percentage of the compositions and preparations may, of course, be varied and may conveniently be between about 5 to about 80% of the weight of the unit. The amount of active compound in such therapeutically useful compositions is such that a suitable dosage will be obtained. Preferred compositions or preparations according to the present invention are prepared so that an oral dosage unit form contains between about 0.01 μg and 10 mg of active compound.

The tablets, troches, pills, capsules and the like may also contain the components as listed hereafter: a binder such as gum, acacia, corn starch or gelatin; excipients such as dicalcium phosphate; a disintegrating agent such as corn starch, potato starch, alginic acid and the like; a lubricant such as magnesium stearate; and a sweetening agent such as sucrose, lactose or saccharin may be added or a flavouring agent such as peppermint, oil of wintergreen, or cherry flavouring. When the dosage unit form is a capsule, it may contain, in addition to materials of the above type, a liquid carrier. Various other materials may be present as coatings or to otherwise modify the physical form of the dosage unit. For instance, tablets, pills, or capsules may be coated with shellac, sugar or both. A syrup or elixir may contain the active compound, sucrose as a sweetening agent, methyl and propylparabens as preservatives, a dye and flavouring such as cherry or orange flavour. Of course, any material used in preparing any dosage unit form should be pharmaceutically pure and substantially non-toxic in the amounts employed. In addition, the active compound(s) may be incorporated into sustained-release preparations and formulations.

The present invention should also be understood to extend to the use of the three-dimensional anti-viral drug-resistant HBV polymerase molecular structure in respect of the analysis and/or elucidation of the nucleic acid replication mechanism of HBV. The present invention further extends to the diagnostic, therapeutic and/or prophylactic developments derived therefrom.

The present invention should still further be understood to extend to any non-naturally occurring form of the anti-viral resistant HBV polymerase molecule. Examples of non-naturally occurring forms of the anti-viral resistant HBV polymerase molecule include inter alia crystallized forms of the molecules.

As indicated above, the present invention contemplates a computer program product for assessing nucleotide sequence differences between a wild-type HBV polymerase and an anti-viral drug-resistant HBV polymerase comprising:

-   (1) code that receives as input values atomic co-ordinates from an     anti-viral drug-resistant HBV polymerase or a fragment thereof; -   (2) code that compares those atomic co-ordinates with the atomic     co-ordinates of a wild-type HBV polymerase or fragment thereof; and -   (3) a computer readable medium that stores the codes.

Still another aspect of the present invention extends to a computer for assessing nucleotide sequence differences between a wild-type HBV polymerase and an anti-viral drug-resistant HBV polymerase comprising:

-   (1) a machine-readable data storage medium comprising a data storage     material encoded with machine-readable data, wherein said     machine-readable data comprise values for the identity of atomic     co-ordinates of wild-type HBV polymerase or a fragment thereof; -   (2) a working memory for storing instructions for processing said     machine-readable data and comparing input data comprising atomic     co-ordinates of an anti-viral drug-resistant HBV polymerase; -   (3) a central-processing unit coupled to said working memory and to     said machine-readable data storage medium, for processing said     machine readable data to compare said values to provide an     assessment of the identity of tags from reference databases; and -   (4) an output hardware coupled to said central processing unit, for     receiving the results of the comparison.

A version of these embodiments is presented in FIG. 7, which shows a system 10 including a computer 11 comprising a central processing unit (“CPU”) 20, a working memory 22 which may be, e.g. RAM (random-access memory) or “core” memory, mass storage memory 24 (such as one or more disk drives or CD-ROM drives), one or more cathode-ray tube (“CRT”) display terminals 26, one or more keyboards 28, one or more input lines 30, and one or more output lines 40, all of which are interconnected by a conventional bidirectional system bus 50.

Input hardware 36, coupled to computer 11 by input lines 30, may be implemented in a variety of ways. For example, machine-readable data of this invention may be inputted via the use of a modem or modems 32 connected by a telephone line or dedicated data line 34. Alternatively or additionally, the input hardware 36 may comprise CD. Alternatively, ROM drives or disk drives 24 in conjunction with display terminal 26, keyboard 28 may also be used as an input device.

Output hardware 46, coupled to computer 11 by output lines 40, may similarly be implemented by conventional devices. By way of example, output hardware 46 may include CRT display terminal 26 for displaying a synthetic polynucleotide sequence or a synthetic polypeptide sequence as described herein. Output hardware might also include a printer 42, so that hard copy output may be produced, or a disk drive 24, to store system output for later use.

In operation, CPU 20 co-ordinates the use of the various input and output devices 36,46 co-ordinates data accesses from mass storage 24 and accesses to and from working memory 22, and determines the sequence of data processing steps. A number of programs may be used to process the machine readable data of this invention.

FIG. 9 shows a cross section of a magnetic data storage medium 100 which can be encoded with machine readable data, or set of instructions, for designing a synthetic molecule of the invention, which can be carried out by a system such as system 10 of FIG. 8. Medium 100 can be a conventional floppy diskette or hard disk, having a suitable substrate 101, which may be conventional, and a suitable coating 102, which may be conventional, on one or both sides, containing magnetic domains (not visible) whose polarity or orientation can be altered magnetically. Medium 100 may also have an opening (not shown) for receiving the spindle of a disk drive or other data storage device 24. The magnetic domains of coating 102 of medium 100 are polarized or oriented so as to encode in manner which may be conventional, machine readable data such as that described herein, for execution by a system such as system 10 of FIG. 8.

FIG. 10 shows a cross section of an optically readable data storage medium 110 which also can be encoded with such a machine-readable data, or set of instructions, for designing a synthetic molecule of the invention, which can be carried out by a system such as system 10 of FIG. 8. Medium 110 can be a conventional compact disk read only memory (CD-ROM) or a rewritable medium such as a magneto-optical disk, which is optically readable and magneto-optically writable. Medium 100 preferably has a suitable substrate 111, which may be conventional, and a suitable coating 112, which may be conventional, usually of one side of substrate 111.

In the case of CD-ROM, as is well known, coating 112 is reflective and is impressed with a plurality of pits 113 to encode the machine-readable data. The arrangement of pits is read by reflecting laser light off the surface of coating 112. A protective coating 114, which preferably is substantially transparent, is provided on top of coating 112.

In accordance with another aspect of the present invention, metal binding sites or regions are identified in the HBV DNA polymerase. Polymerase molecules require metal ions for catalysis. Two magnesium ions are required in the HIV polymerase and these are located near the aspartic acid residues 185 and 186. In addition to this metal binding region (defined by residues 205 and 206 in the present model), according to the present invention, three regions are identified containing clusters of histidine and cysteine residues.

These regions are defined by the amino acid residues selected from the list comprising: Metal Binding Site 1: rtE1, rtH12, rtH13, rtH160 and rtA162; Metal Binding Site 2: rtC-9, rtH-6, rtH90, rtL93, rtH234; Metal Binding Site 3: rtH197, rtC198, rtH216 and rtC213.

These metal binding sites are also shown in FIGS. 17, 18 and 19.

It has been previously demonstrated in other polymerase proteins that cysteine and histidine residues have an effect on metal-ion preference and are important for activity in that they affect the sensitivity and magnitude of induction. (Khan et al., Biochem Biophys Res Commun. 299(3):438-45, 2002; Wulfing et al., J Biol. Chem. 269(4):2895-901, 1994). These new binding sites are proposed to be involved in polymerase activity or associated functions such as RNA/DNA binding or strand transfer of the newly elongated strand. These additional metal binding sites for the HBV polymerase have not been previously identified are targets for antiviral compounds or diagnostic agents.

Accordingly, another aspect of the present invention is directed to an isolated fragment of an HBV polymerase comprising amino acid residues selected from (i) rtE1, rtH12, rtH13, rtH160, rtA162; (ii) rtC-9, rtH-6, rtH90, rtL93, rtH234; and (iii) rtH197, rtC198, rtH216 and rtC213, wherein said fragment is capable of binding a metal ion as shown in FIGS. 17, 18 and 19 and wherein said fragment is capable of binding a metal ion.

A further embodiment contemplates a method for screening for an anti-HBV agent or diagnostic agent said method comprising identifying a compound which is capable of binding, assocaiting with or otherwise interactng with a region of an HBV polymerase defind by amino acid residues selected from (i) rtE1, rtH12, rtH13, rtH160 and rtA162; (ii) rtC-9, rtH-6, rtH90, rtL93, rtH234; and (iii) rtH197, rtC198, rtH216 and rtC213 wherein said region is a metal ion binding site as shown in FIGS. 17, 18 and 19.

Anti-HBV agents identified according to this method may be used in a vaccine or as a diagnostic agent. In relation to the latter embodiment, a diagnostic agent is provided comprising a molecule capable of binding, associating with or interacting with a region of an HBV polymerase defined at or near amino acid residues selected from (i) rtE1, rtH12, rtH13, rtH160 and rtA162; (ii) rtC-9, rtH-6, rtH90, rtL93, rtH234; and (iii) rtH197, rtC198, rtH216 and rtC213, wherein said region is a metal ion binding site as shown in FIGS. 17, 18 and 19 wherein said region is a metal ion binding site. As a diagnostic agent, the agent may be labeled directly with a reporter molecule capable of providing an identifiable signal or the agent may be identified by use of, for example, antibodies or other ligands of the agent.

The present invention further provides the use of metal ion binding sites in the HBV DNA polymerase in the identification of an HBV binding agent or a metal ion binding-inhibiting agent in the manufacture of a medicament or diagnostic agent for the treatment or detection of HBV infection.

The present invention is further described by the following non-limiting examples.

EXAMPLE 1 Molecular Modeling of HBV Polymerase

HBV polymerase models were constructed using the crystal structures of human immunodeficiency virus (HIV) reverse transcriptase (1RTD) reported by Das et al., 2001, supra and moloney murine leukemia virus (MMLV) reverse transcriptase (1MML) by Georgiadis M M, Jessen S M, Ogata C M, Telesnitsky A, Goff S P, Hendrickson W A., Structure 3: 879, 1995 as the template for homology modeling.

The initial sequence alignment of HBV polymerase of sequence number −25 to 299 against HIV RT and MMLV RT was originally generated with ClustalW (Thompson J. D., Higgins, D. G. and Gibson, T. J. Nucleic Acids Research, 1994 22:4673-4680) using a BLOSUM 62 matrix followed by further manual alignment.

Secondary structure predictions of the HBV polymerase was based on the consensus of five independent secondary structure prediction algorithms: GORIV (Garnier J, Gibrat J-F, Robson B Methods in Enzymology 1996 R. F. Doolittle Ed., vol 266, 540-553), PHD (Rost B, Sander C Proc Natl Acad Sci USA. 1993 Aug. 15; 90(16):7558-62.), PsiPred (Jones D T. (1999), J. Mol. Biol. 292: 195-202), Sspro (G. Pollastri, D. Przybylski, B. Rost, and P. Baldi, Proteins, 47(2):228-235, 2002.), and SOMPA (Geourjon C, Deleage G, Comput Appl Biosci 1995 December; 11(6):681-684.).

Homology models of HBV polymerase were constructed manually using Sybyl6.9 (Tripos Sybyl; version 6.9 ed: 1699 South Hanley Road, St Louis, Mo. 63144, USA) such that regions of high sequence identity to the HIV and MMLV RT shared the same backbone conformation while flanking regions were modeled consistant with secondary structure predictions. A double stranded DNA molecule was also included before the model was further geometrically optimised using molecular dynamics simulations in Sybyl. Drug molecules were manually docked into the model with changes made to the complementary strand of DNA such that optimal base pairing could still occur. Molecular models were solvated in a 81 angstrom cube of water and subjected to NAMD molecular dynamics simulations (L Kale, R Skeel, M Bhandarkar, R Brunner, A Gursoy, N Krawetz, J Phillips, A Shinozaki, K Varadarajan, and K Schulten. Journal of Computational Physics, 151:283-312, 1999) for 1 nanosecond for a final structural equilibration.

EXAMPLE 2 HBV Polymerase

The molecular model of an HBV polymerase was determined. The model is shown in FIG. 2.

EXAMPLE 3 Atomic Co-Ordinates

The atomic co-ordinates of the HBV polymerase are shown in Table 6.

EXAMPLE 4 LMV Resistance

L180M and M204 V and L180M and M204I

L180 has been mutated to methionine and M204 has been mutated to valine (FIG. 4). This steric hindrance gives rise to the resistance of LMV as it can no longer bind tightly in the binding site. The same effect is seen when M204 is mutated to isoleucine.

L80I

The leucine 80 mutation to isoleucine is a relatively conservative mutation, however, the branching of isoleucine at the β carbon as opposed to the γ carbon restricts the movement of this residue and reduces its backbone flexibility in comparison to leucine. As Leu80 is located in the junction of palm/thumb region of the binding site, it would be involved in some flexing of the binding site, the reduced flexing ability that isoleucine would possess compared to leucine may explain in part some of the drug resistance arising from this mutation. The results are shown in FIG. 10.

V173L

The mutation of valine 173 to Leucine alters the shape of the binding site by interacting with the phenylalanine 88, which forms part of the binding site. The additional space taken up by the larger leucine causes the aromatic ring of the phenylalanine to rotate further into the cavity of the bind site and thus altering the binding sites shape. It is proposed that this modification in the shape of the binding site gives rise to drug resistance. The results are shown in FIG. 11.

EXAMPLE 5 ADV Resistance

A181T

The alanine 181 mutation to threonine enables an additional hydrogen bond to be formed between the hydroxyl portion of threonine and the carbonyl oxygen of proline 177. This additional hydrogen bond will cause the helix, which is part of domain B, to bend and thus alter the shape of the binding site. This altered shape of the binding site is proposed to give rise to drug resistance. The results are shown in FIG. 12.

N236T

The mutation of asparagine 236 to threonine will result in the loss of a hydrogen bond between 236 and serine 85. The loss of this hydrogen bond may result in the binding site changing shape. In addition to this possible modification of the binding site serine 85 is directly involved in the binding of nucleoside inhibitors via a hydrogen bond to the y phosphate group. Thus the mutation of Asn 236 to Thr 236 may give rise to drug resistance via modifications of the binding site. The results are shown in FIG. 13.

EXAMPLE 6 ETV Resistance

A38E

The mutation of alanine 38 to glutamic acid would alter the shape of domain F, which is involved in the binding of the nucleoside. As there is already a high concentration of negatively charged residues in domain F, additional negatively charged residues would hinder the binding of ETV due to unfavourable negative/negative charge interactions between these residues and the negatively charged phosphate groups. The results are shown in FIG. 14.

T184G

This mutation is similar to the A181T mutation in that both mutations result in a change in the bend of the helix. The highly flexible glycine residue enables the helix in domain B to bend to a much greater extent which in turn modifies the binding site of the nucleosides, resulting in drug resistance.

S202I

The mutation of serine 202 to isoleucine could cause a number of changes due to the much greater space that the isoleucine requires. The isoleucine 202 mutant occupies additional space between domains B and C where it is not present in the wild-type virus. The additional space isoleucine 202 requires causes slight movements of domain C up and domain B down; this in turn alters the binding site which gives rise to drug resistance. The results are shown in FIG. 15.

M250V

The methionine 250 to valine mutation is located at the turn in domain E that is in close proximity to the nucleoside-binding site. It is thought that this mutation will affect the packing of residues in the vicinity of the binding site and thus give rise to drug resistance.

EXAMPLE 7 Identification of Metal Binding Sites in HBV Polymerase

Polymerase molecules require metal ions for catalysis. Two magnesium ions are required in the HIV polymerase and these are located near the aspartic acid residues 185 and 186. In addition to this metal binding region (defined by residues 205 and 206 in the present model) three further regions are identified containing clusters of histidine and cysteine residues. It has been previously demonstrated in other polymerase proteins that cysteine and histidine residues have an effect on metal-ion preference and are important for activity in that they affect the sensitivity and magnitude of induction. (Khan et al., Biochem Biophys Res Commun. 299(3):438-45, 2002; Wulfing et al., J Biol. Chem. 269(4):2895-901, 1994). The proposed metal binding sites in the HBV polymerase model are shown in FIGS. 17, 18 and 19. Metal binding Site 1 includes residues rtE1, rtH12, rtH13 rtH160 and rtA162. Metal binding Site 2 includes residues rtC-9, rtH-6, rtH90, rtL93 and rtH234. Metal binding Site 3 includes residues rtH197, rtC198, rtH216 and rtC213. These new binding sites may be involved in polymerase activity or associated functions such as RNA/DNA binding or strand transfer of the newly elongated strand. These additional metal binding sites for the HBV polymerase have not been previously identified and may be targets for antiviral compounds.

EXAMPLE 8 In Vitro Resistance Testing

The mutation rtS85A was chosen to test in an antiviral resistance testing assay due to (a) it proposed location near rtN236T and the tri-phosphate binding site in a homology model of the HBV polymerase (b) This mutation was detected in HBV isolated from a patient not on ADV suggesting that this mutation could exist as a dominate replicating species in a patient

(a) Creation of Mutations by Site-Directed Mutagenesis in the HBV Infectious Clone

The plasmid containing 1.3×HBV genome in the vector pBlueBac4.5 was used as the infectious HBV clone. This clone already had the precore mutation at G1896A. The point mutation were created by site directed mutagenesis using the commercial kits according to the manufacturers specifications (QuikChange, Stratagene). A HBV recombinant encoding the reverse transcriptase mutations rtS85A was created. The nucleotide sequence of the plasmid and the point mutations generated by site directed mutagenesis were confirmed by sequencing using the ABI Prism Big Dye Terminator Cycle Sequencing Ready Reaction Kit according to the manufacturer's specifications (Perkin Elmer, Cetus Norwalk, Conn.).

(b) Transfection of HepG2 Cells with Plasmid DNA and Antiviral Treatments

Huh7 cells were seeded at approximately 20-40% confluency and then were grown for 16-24 hours before transfection. Plasmid DNA containing HBV encoding specific mutations was transfected using Fugene according to the manufacturers protocols.

ADV and LMV were resuspended in sterile water, aliquoted, and frozen at −20° C. to avoid repeated freezing and thawing of the drug. Medium containing ADV or LMV were prepared daily as needed. In experiments in which ADV or LMV treatment was initiated 2 hr prior to transfection, Huh7 cells were exposed to the indicated concentration of ADV or LMV immediately after transfection with the HBV plasmid.

(c) Analysis of HBV Replicative Intermediates

Analysis of Secreted HBV Antigen

Detection of hepatitis Be antigen (HBeAg) and hepatitis B surface antigen (HBsAg) were performed by radioimmunoassay and microparticle enzyme immunoassay using kits purchased from Abbott Laboratories (Abbott Park, Ill., USA). Medium from Huh7 cells was collected, centrifuged at 6,000 g to remove cellular debris, transferred to clean tubes, and stored at 20° C. until analysis. HBeAg and HBsAg values are expressed as fold of positive control. Medium samples were diluted appropriately so that radioimmunassay results were below positive control values for HBeAg or HBsAg, respectively.

Detection of Intracellular Replicative Intermediates

HBV core particles were isolated from the cytoplasmic fraction of Huh7 cells lysis buffer which includes 0.5% w/v NP-40. Cytoplasmic extracts were treated with DNAse, adjusted to 10 mmol/l McCl2 and unprotected DNA was removed by an incubation to 500 g/ml Proteinase K for 1.5 hours at 37° C. HBV DNA in the samples were then extracted using commercial DNA extraction kits such as Qiagen (DNA extraction) or in-house methods using sequential phenol and chloroform extractions, and the nucleic acids were recovered by ethanol precipitation. Nucleic acids were resuspended in 50 μl/1 TE (10 mmol/l Tris, 1 mmol/l ethylenediaminetetraacetic acid) or 5 mmol/l ethylenediaminetetraacetic acid, normalized by OD260, before analysis by electrophoresis and Southern blotting. After southern blot analysis a BioRad Phosphoimager and the Quantity One Analysis software (BioRad, Hecules Calif.) was used to analyze suitable exposures of Southern blots. Densitometry data was fitted to logistic dose response curves using the TableCurve 2D software package from Jandel Scientific. Logistic dose response equations were used to calculate IC₅₀ and IC₉₀ values and co-efficients of variation.

Antiviral Testing Performed with HBV Plasmid Encoding rtS85A

The dose effect of ADV and LMV on HBV encoding rtS85A is shown in FIG. 21 using the ADV (0 μM) and LMV (0 μM) as controls, There was reduced sensitivity to ADV by the recombinant HBV encoding the mutant rtS85A. The HBV precore mutant has an IC50 of 0.43 μM for ADV and an IC50 for LMV at 0.005 μM. In contrast, the mutant encoding the additional rtS85A had an IC50 for LMV at 0.01 μM and between 5-10 μM for ADV. TABLE 6 Atomic co-ordinates HBV polymerase model_040504_a1 ATOM 1 N GLY A 975 9.098 −21.241 2.066 1.00 1.00 N ATOM 2 CA GLY A 975 8.102 −20.156 1.866 1.00 1.00 C ATOM 3 C GLY A 975 8.475 −19.295 0.703 1.00 1.00 C ATOM 4 O GLY A 975 9.547 −19.538 0.180 1.00 1.00 O ATOM 5 HA2 GLY A 975 8.160 −19.464 2.700 1.00 1.00 H ATOM 6 HA1 GLY A 975 7.068 −20.429 1.711 1.00 1.00 H ATOM 7 HN GLY A 975 10.068 −21.038 2.032 1.00 1.00 H ATOM 8 H GLY A 975 8.831 −22.032 2.624 1.00 1.00 H ATOM 9 N PRO A 976 7.694 −18.239 0.381 1.00 1.00 N ATOM 10 CA PRO A 976 8.239 −17.093 −0.391 1.00 1.00 C ATOM 11 C PRO A 976 9.103 −16.394 0.644 1.00 1.00 C ATOM 12 O PRO A 976 8.839 −15.286 1.103 1.00 1.00 O ATOM 13 CB PRO A 976 6.968 −16.248 −0.736 1.00 1.00 C ATOM 14 CG PRO A 976 6.153 −16.498 0.584 1.00 1.00 C ATOM 15 CD PRO A 976 6.316 −18.040 0.847 1.00 1.00 C ATOM 16 HA PRO A 976 8.746 −17.334 −1.341 1.00 1.00 H ATOM 17 HD2 PRO A 976 5.743 −18.680 0.172 1.00 1.00 H ATOM 18 HD1 PRO A 976 6.032 −18.268 1.873 1.00 1.00 H ATOM 19 HG2 PRO A 976 5.092 −16.273 0.332 1.00 1.00 H ATOM 20 HG1 PRO A 976 6.431 −15.956 1.524 1.00 1.00 H ATOM 21 HB1 PRO A 976 6.340 −16.596 −1.618 1.00 1.00 H ATOM 22 HB2 PRO A 976 7.130 −15.172 −0.885 1.00 1.00 H ATOM 23 N CYS A 977 10.213 −17.040 1.020 1.00 1.00 N ATOM 24 CA CYS A 977 10.934 −16.779 2.278 1.00 1.00 C ATOM 25 C CYS A 977 11.315 −18.145 2.923 1.00 1.00 C ATOM 26 O CYS A 977 10.624 −19.138 2.692 1.00 1.00 O ATOM 27 CB CYS A 977 10.232 −16.076 3.452 1.00 1.00 C ATOM 28 SG CYS A 977 8.579 −16.705 3.742 1.00 1.00 S ATOM 29 HA CYS A 977 11.884 −16.200 2.086 1.00 1.00 H ATOM 30 HB1 CYS A 977 10.119 −15.007 3.159 1.00 1.00 H ATOM 31 HB2 CYS A 977 10.873 −16.007 4.345 1.00 1.00 H ATOM 32 HG CYS A 977 8.328 −16.030 4.413 1.00 1.00 H ATOM 33 HN CYS A 977 10.586 −17.761 0.446 1.00 1.00 H ATOM 34 N TRP A 978 12.404 −18.253 3.753 1.00 1.00 N ATOM 35 CA TRP A 978 12.903 −19.526 4.280 1.00 1.00 C ATOM 36 C TRP A 978 12.971 −19.279 5.751 1.00 1.00 C ATOM 37 O TRP A 978 14.045 −19.317 6.312 1.00 1.00 O ATOM 38 CB TRP A 978 14.210 −19.696 3.508 1.00 1.00 C ATOM 39 CG TRP A 978 13.858 −19.779 2.007 1.00 1.00 C ATOM 40 CD1 TRP A 978 14.255 −18.931 1.034 1.00 1.00 C ATOM 41 CD2 TRP A 978 13.135 −20.910 1.361 1.00 1.00 C ATOM 42 NE1 TRP A 978 13.746 −19.324 −0.125 1.00 1.00 N ATOM 43 CE2 TRP A 978 13.011 −20.448 0.067 1.00 1.00 C ATOM 44 CE3 TRP A 978 12.659 −22.140 1.784 1.00 1.00 C ATOM 45 CZ2 TRP A 978 12.224 −21.127 −0.872 1.00 1.00 C ATOM 46 CZ3 TRP A 978 11.866 −22.882 0.854 1.00 1.00 C ATOM 47 CH2 TRP A 978 11.660 −22.335 −0.450 1.00 1.00 C ATOM 48 HA TRP A 978 12.303 −20.426 4.162 1.00 1.00 H ATOM 49 HB1 TRP A 978 14.781 −20.559 3.898 1.00 1.00 H ATOM 50 HB2 TRP A 978 14.787 −18.761 3.703 1.00 1.00 H ATOM 51 HE1 TRP A 978 13.851 −18.871 −1.036 1.00 1.00 H ATOM 52 HD1 TRP A 978 14.890 −18.065 1.234 1.00 1.00 H ATOM 53 HZ2 TRP A 978 12.028 −20.755 −1.865 1.00 1.00 H ATOM 54 HH2 TRP A 978 11.070 −22.901 −1.196 1.00 1.00 H ATOM 55 HZ3 TRP A 978 11.510 −23.880 1.096 1.00 1.00 H ATOM 56 HE3 TRP A 978 12.886 −22.518 2.785 1.00 1.00 H ATOM 57 HN TRP A 978 12.874 −17.448 4.099 1.00 1.00 H ATOM 58 N TRP A 979 11.812 −18.977 6.404 1.00 1.00 N ATOM 59 CA TRP A 979 11.780 −18.720 7.806 1.00 1.00 C ATOM 60 C TRP A 979 10.375 −18.911 8.325 1.00 1.00 C ATOM 61 O TRP A 979 9.652 −19.534 7.591 1.00 1.00 O ATOM 62 CB TRP A 979 12.411 −17.325 8.050 1.00 1.00 C ATOM 63 CG TRP A 979 11.563 −16.098 7.828 1.00 1.00 C ATOM 64 CD1 TRP A 979 10.474 −15.996 7.075 1.00 1.00 C ATOM 65 CD2 TRP A 979 11.906 −14.754 8.421 1.00 1.00 C ATOM 66 NE1 TRP A 979 10.179 −14.746 7.060 1.00 1.00 N ATOM 67 CE2 TRP A 979 10.933 −13.967 7.829 1.00 1.00 C ATOM 68 CE3 TRP A 979 12.887 −14.240 9.249 1.00 1.00 C ATOM 69 CZ2 TRP A 979 10.853 −12.583 8.059 1.00 1.00 C ATOM 70 CZ3 TRP A 979 12.875 −12.856 9.348 1.00 1.00 C ATOM 71 CH2 TRP A 979 11.857 −12.015 8.842 1.00 1.00 C ATOM 72 HA TRP A 979 12.390 −19.555 8.245 1.00 1.00 H ATOM 73 HB1 TRP A 979 13.281 −17.243 7.359 1.00 1.00 H ATOM 74 HB2 TRP A 979 12.885 −17.287 9.026 1.00 1.00 H ATOM 75 HE1 TRP A 979 9.422 −14.396 6.502 1.00 1.00 H ATOM 76 HD1 TRP A 979 10.001 −16.788 6.498 1.00 1.00 H ATOM 77 HZ2 TRP A 979 10.044 −12.046 7.630 1.00 1.00 H ATOM 78 HH2 TRP A 979 11.868 −10.941 9.048 1.00 1.00 H ATOM 79 HZ3 TRP A 979 13.717 −12.380 9.866 1.00 1.00 H ATOM 80 HE3 TRP A 979 13.638 −14.910 9.707 1.00 1.00 H ATOM 81 HN TRP A 979 10.934 −18.878 5.904 1.00 1.00 H ATOM 82 N LEU A 980 9.949 −18.352 9.492 1.00 1.00 N ATOM 83 CA LEU A 980 8.536 −18.570 9.907 1.00 1.00 C ATOM 84 C LEU A 980 7.678 −17.767 8.911 1.00 1.00 C ATOM 85 O LEU A 980 8.165 −16.797 8.351 1.00 1.00 O ATOM 86 CB LEU A 980 8.093 −18.124 11.304 1.00 1.00 C ATOM 87 CG LEU A 980 8.558 −19.071 12.431 1.00 1.00 C ATOM 88 CD1 LEU A 980 7.859 −20.460 12.488 1.00 1.00 C ATOM 89 CD2 LEU A 980 10.106 −19.229 12.414 1.00 1.00 C ATOM 90 HA LEU A 980 8.217 −19.654 9.833 1.00 1.00 H ATOM 91 HB1 LEU A 980 7.002 −18.077 11.361 1.00 1.00 H ATOM 92 HB2 LEU A 980 8.499 −17.104 11.459 1.00 1.00 H ATOM 93 HG LEU A 980 8.335 −18.497 13.389 1.00 1.00 H ATOM 94 HD21 LEU A 980 10.686 −18.251 12.496 1.00 1.00 H ATOM 95 HD22 LEU A 980 10.412 −19.746 11.469 1.00 1.00 H ATOM 96 HD23 LEU A 980 10.400 −19.792 13.299 1.00 1.00 H ATOM 97 HD11 LEU A 980 6.770 −20.393 12.300 1.00 1.00 H ATOM 98 HD12 LEU A 980 8.089 −20.994 13.463 1.00 1.00 H ATOM 99 HD13 LEU A 980 8.273 −21.106 11.703 1.00 1.00 H ATOM 100 HN LEU A 980 10.501 −17.727 10.060 1.00 1.00 H ATOM 101 N GLN A 981 6.356 −18.115 8.799 1.00 1.00 N ATOM 102 CA GLN A 981 5.528 −17.601 7.675 1.00 1.00 C ATOM 103 C GLN A 981 4.223 −17.145 8.243 1.00 1.00 C ATOM 104 O GLN A 981 3.245 −17.266 7.532 1.00 1.00 O ATOM 105 CB GLN A 981 5.310 −18.750 6.639 1.00 1.00 C ATOM 106 CG GLN A 981 6.619 −19.544 6.286 1.00 1.00 C ATOM 107 CD GLN A 981 6.335 −20.618 5.259 1.00 1.00 C ATOM 108 OE1 GLN A 981 6.635 −20.365 4.105 1.00 1.00 O ATOM 109 NE2 GLN A 981 5.814 −21.810 5.657 1.00 1.00 N ATOM 110 HA GLN A 981 5.976 −16.723 7.194 1.00 1.00 H ATOM 111 HB1 GLN A 981 4.962 −18.353 5.657 1.00 1.00 H ATOM 112 HB2 GLN A 981 4.561 −19.485 6.957 1.00 1.00 H ATOM 113 HG1 GLN A 981 7.096 −19.978 7.189 1.00 1.00 H ATOM 114 HG2 GLN A 981 7.383 −18.836 5.880 1.00 1.00 H ATOM 115 HE22 GLN A 981 5.601 −22.529 4.974 1.00 1.00 H ATOM 116 HE21 GLN A 981 5.512 −22.039 6.591 1.00 1.00 H ATOM 117 HN GLN A 981 5.961 −18.762 9.399 1.00 1.00 H ATOM 118 N PHE A 982 4.105 −16.633 9.472 1.00 1.00 N ATOM 119 CA PHE A 982 2.784 −16.333 10.045 1.00 1.00 C ATOM 120 C PHE A 982 2.726 −15.137 10.982 1.00 1.00 C ATOM 121 O PHE A 982 2.312 −15.283 12.123 1.00 1.00 O ATOM 122 CB PHE A 982 2.224 −17.590 10.765 1.00 1.00 C ATOM 123 CG PHE A 982 2.227 −18.789 9.742 1.00 1.00 C ATOM 124 CD1 PHE A 982 1.206 −18.844 8.816 1.00 1.00 C ATOM 125 CD2 PHE A 982 3.225 −19.759 9.780 1.00 1.00 C ATOM 126 CE1 PHE A 982 1.288 −19.743 7.747 1.00 1.00 C ATOM 127 CE2 PHE A 982 3.160 −20.822 8.855 1.00 1.00 C ATOM 128 CZ PHE A 982 2.212 −20.803 7.821 1.00 1.00 C ATOM 129 HA PHE A 982 2.169 −16.042 9.196 1.00 1.00 H ATOM 130 HB1 PHE A 982 1.207 −17.356 11.119 1.00 1.00 H ATOM 131 HB2 PHE A 982 2.838 −17.955 11.617 1.00 1.00 H ATOM 132 HD2 PHE A 982 4.060 −19.775 10.510 1.00 1.00 H ATOM 133 HE2 PHE A 982 3.844 −21.670 8.866 1.00 1.00 H ATOM 134 HZ PHE A 982 2.191 −21.608 7.073 1.00 1.00 H ATOM 135 HE1 PHE A 982 0.618 −19.693 6.890 1.00 1.00 H ATOM 136 HD1 PHE A 982 0.356 −18.149 8.915 1.00 1.00 H ATOM 137 HN PHE A 982 4.885 −16.435 10.024 1.00 1.00 H ATOM 138 N ARG A 983 2.979 −13.908 10.540 1.00 1.00 N ATOM 139 CA ARG A 983 2.796 −12.715 11.368 1.00 1.00 C ATOM 140 C ARG A 983 1.340 −12.382 11.184 1.00 1.00 C ATOM 141 O ARG A 983 1.082 −11.344 10.610 1.00 1.00 O ATOM 142 CB ARG A 983 3.793 −11.545 11.056 1.00 1.00 C ATOM 143 CG ARG A 983 5.246 −11.751 11.711 1.00 1.00 C ATOM 144 CD ARG A 983 6.078 −12.805 10.867 1.00 1.00 C ATOM 145 NE ARG A 983 7.506 −12.891 11.153 1.00 1.00 N ATOM 146 CZ ARG A 983 8.378 −13.721 10.578 1.00 1.00 C ATOM 147 NH1 ARG A 983 8.002 −14.619 9.726 1.00 1.00 N ATOM 148 NH2 ARG A 983 9.624 −13.679 10.845 1.00 1.00 N ATOM 149 HA ARG A 983 2.885 −12.968 12.437 1.00 1.00 H ATOM 150 HB1 ARG A 983 3.335 −10.663 11.481 1.00 1.00 H ATOM 151 HB2 ARG A 983 3.883 −11.340 9.959 1.00 1.00 H ATOM 152 HG1 ARG A 983 5.151 −12.042 12.764 1.00 1.00 H ATOM 153 HG2 ARG A 983 5.836 −10.850 11.621 1.00 1.00 H ATOM 154 HD1 ARG A 983 6.046 −12.546 9.805 1.00 1.00 H ATOM 155 HD2 ARG A 983 5.652 −13.830 11.091 1.00 1.00 H ATOM 156 HE ARG A 983 7.841 −12.217 11.851 1.00 1.00 H ATOM 157 HH12 ARG A 983 8.675 −15.220 9.280 1.00 1.00 H ATOM 158 HH11 ARG A 983 7.057 −14.760 9.402 1.00 1.00 H ATOM 159 HH22 ARG A 983 10.306 −14.333 10.437 1.00 1.00 H ATOM 160 HH21 ARG A 983 9.927 −13.118 11.581 1.00 1.00 H ATOM 161 HN ARG A 983 3.300 −13.774 9.618 1.00 1.00 H ATOM 162 N ASN A 984 0.370 −13.280 11.623 1.00 1.00 N ATOM 163 CA ASN A 984 −1.048 −12.964 11.440 1.00 1.00 C ATOM 164 C ASN A 984 −1.253 −11.669 12.172 1.00 1.00 C ATOM 165 O ASN A 984 −0.487 −11.361 13.084 1.00 1.00 O ATOM 166 CB ASN A 984 −1.992 −14.031 12.086 1.00 1.00 C ATOM 167 CG ASN A 984 −1.687 −15.381 11.509 1.00 1.00 C ATOM 168 OD1 ASN A 984 −0.957 −16.111 12.155 1.00 1.00 O ATOM 169 ND2 ASN A 984 −2.127 −15.663 10.252 1.00 1.00 N ATOM 170 HA ASN A 984 −1.166 −12.815 10.323 1.00 1.00 H ATOM 171 HB1 ASN A 984 −3.041 −13.772 11.961 1.00 1.00 H ATOM 172 HB2 ASN A 984 −1.801 −14.115 13.177 1.00 1.00 H ATOM 173 HD22 ASN A 984 −1.772 −16.510 9.835 1.00 1.00 H ATOM 174 HD21 ASN A 984 −2.660 −15.012 9.719 1.00 1.00 H ATOM 175 HN ASN A 984 0.608 −14.108 12.210 1.00 1.00 H ATOM 176 N SER A 985 −2.310 −10.838 11.864 1.00 1.00 N ATOM 177 CA SER A 985 −2.464 −9.571 12.582 1.00 1.00 C ATOM 178 C SER A 985 −3.890 −9.044 12.469 1.00 1.00 C ATOM 179 O SER A 985 −4.570 −8.908 13.484 1.00 1.00 O ATOM 180 CB SER A 985 −1.550 −8.495 12.070 1.00 1.00 C ATOM 181 OG SER A 985 −1.775 −8.276 10.692 1.00 1.00 O ATOM 182 HA SER A 985 −2.364 −9.676 13.679 1.00 1.00 H ATOM 183 HB1 SER A 985 −0.497 −8.698 12.362 1.00 1.00 H ATOM 184 HB2 SER A 985 −1.799 −7.533 12.509 1.00 1.00 H ATOM 185 HG SER A 985 −1.421 −9.033 10.207 1.00 1.00 H ATOM 186 HN SER A 985 −2.933 −11.139 11.181 1.00 1.00 H ATOM 187 N LYS A 986 −4.472 −8.771 11.259 1.00 1.00 N ATOM 188 CA LYS A 986 −5.841 −8.195 11.267 1.00 1.00 C ATOM 189 C LYS A 986 −6.890 −9.331 11.210 1.00 1.00 C ATOM 190 O LYS A 986 −6.565 −10.364 10.644 1.00 1.00 O ATOM 191 CB LYS A 986 −6.052 −7.401 9.923 1.00 1.00 C ATOM 192 CG LYS A 986 −5.447 −5.985 10.068 1.00 1.00 C ATOM 193 CD LYS A 986 −3.901 −6.078 10.176 1.00 1.00 C ATOM 194 CE LYS A 986 −3.139 −4.722 9.880 1.00 1.00 C ATOM 195 NZ LYS A 986 −3.423 −3.698 10.894 1.00 1.00 N ATOM 196 HA LYS A 986 −6.043 −7.510 12.083 1.00 1.00 H ATOM 197 HB1 LYS A 986 −5.699 −7.987 9.129 1.00 1.00 H ATOM 198 HB2 LYS A 986 −7.168 −7.243 9.805 1.00 1.00 H ATOM 199 HG1 LYS A 986 −5.756 −5.471 10.982 1.00 1.00 H ATOM 200 HG2 LYS A 986 −5.724 −5.419 9.167 1.00 1.00 H ATOM 201 HD1 LYS A 986 −3.598 −6.761 9.353 1.00 1.00 H ATOM 202 HD2 LYS A 986 −3.593 −6.452 11.162 1.00 1.00 H ATOM 203 HE1 LYS A 986 −3.490 −4.323 8.919 1.00 1.00 H ATOM 204 HE2 LYS A 986 −2.078 −4.881 9.845 1.00 1.00 H ATOM 205 HZ1 LYS A 986 −3.115 −2.702 10.657 1.00 1.00 H ATOM 206 HZ2 LYS A 986 −2.954 −3.856 11.827 1.00 1.00 H ATOM 207 HZ3 LYS A 986 −4.500 −3.527 10.979 1.00 1.00 H ATOM 208 HN LYS A 986 −4.013 −8.934 10.416 1.00 1.00 H ATOM 209 N PRO A 987 −8.126 −9.236 11.778 1.00 1.00 N ATOM 210 CA PRO A 987 −9.006 −10.400 11.720 1.00 1.00 C ATOM 211 C PRO A 987 −9.613 −10.588 10.350 1.00 1.00 C ATOM 212 O PRO A 987 −10.763 −10.220 10.160 1.00 1.00 O ATOM 213 CB PRO A 987 −9.915 −10.077 12.949 1.00 1.00 C ATOM 214 CG PRO A 987 −10.027 −8.545 12.833 1.00 1.00 C ATOM 215 CD PRO A 987 −8.590 −8.066 12.478 1.00 1.00 C ATOM 216 HA PRO A 987 −8.450 −11.343 11.970 1.00 1.00 H ATOM 217 HD2 PRO A 987 −8.531 −7.158 11.853 1.00 1.00 H ATOM 218 HD1 PRO A 987 −7.999 −8.031 13.403 1.00 1.00 H ATOM 219 HG2 PRO A 987 −10.367 −8.061 13.786 1.00 1.00 H ATOM 220 HG1 PRO A 987 −10.725 −8.284 11.979 1.00 1.00 H ATOM 221 HB1 PRO A 987 −9.293 −10.308 13.848 1.00 1.00 H ATOM 222 HB2 PRO A 987 −10.875 −10.546 13.010 1.00 1.00 H ATOM 223 N CYS A 988 −8.819 −11.183 9.400 1.00 1.00 N ATOM 224 CA CYS A 988 −9.371 −11.366 7.995 1.00 1.00 C ATOM 225 C CYS A 988 −9.853 −10.019 7.328 1.00 1.00 C ATOM 226 O CYS A 988 −9.225 −9.570 6.395 1.00 1.00 O ATOM 227 CB CYS A 988 −10.478 −12.406 7.852 1.00 1.00 C ATOM 228 SG CYS A 988 −9.925 −14.093 7.858 1.00 1.00 S ATOM 229 HA CYS A 988 −8.585 −11.752 7.376 1.00 1.00 H ATOM 230 HB1 CYS A 988 −10.883 −12.287 6.861 1.00 1.00 H ATOM 231 HB2 CYS A 988 −11.233 −12.178 8.622 1.00 1.00 H ATOM 232 HG CYS A 988 −10.804 −14.532 7.549 1.00 1.00 H ATOM 233 HN CYS A 988 −7.862 −11.354 9.618 1.00 1.00 H ATOM 234 N SER A 989 −10.944 −9.439 7.817 1.00 1.00 N ATOM 235 CA SER A 989 −11.548 −8.248 7.159 1.00 1.00 C ATOM 236 C SER A 989 −11.700 −8.450 5.645 1.00 1.00 C ATOM 237 O SER A 989 −12.801 −8.795 5.247 1.00 1.00 O ATOM 238 CB SER A 989 −10.678 −7.018 7.508 1.00 1.00 C ATOM 239 OG SER A 989 −10.707 −6.766 8.937 1.00 1.00 O ATOM 240 HA SER A 989 −12.526 −8.132 7.678 1.00 1.00 H ATOM 241 HB1 SER A 989 −11.273 −6.158 7.107 1.00 1.00 H ATOM 242 HB2 SER A 989 −9.661 −7.017 7.080 1.00 1.00 H ATOM 243 HG SER A 989 −10.409 −7.536 9.410 1.00 1.00 H ATOM 244 HN SER A 989 −11.357 −9.790 8.665 1.00 1.00 H ATOM 245 N ASP A 990 −10.653 −8.340 4.750 1.00 1.00 N ATOM 246 CA ASP A 990 −10.799 −8.615 3.268 1.00 1.00 C ATOM 247 C ASP A 990 −9.684 −9.479 2.765 1.00 1.00 C ATOM 248 O ASP A 990 −9.266 −9.300 1.629 1.00 1.00 O ATOM 249 CB ASP A 990 −10.994 −7.278 2.552 1.00 1.00 C ATOM 250 CG ASP A 990 −11.870 −7.403 1.302 1.00 1.00 C ATOM 251 OD1 ASP A 990 −13.139 −7.167 1.381 1.00 1.00 O ATOM 252 OD2 ASP A 990 −11.324 −7.833 0.273 1.00 1.00 O ATOM 253 HA ASP A 990 −11.682 −9.234 3.115 1.00 1.00 H ATOM 254 HB1 ASP A 990 −10.020 −6.828 2.325 1.00 1.00 H ATOM 255 HB2 ASP A 990 −11.585 −6.562 3.234 1.00 1.00 H ATOM 256 HN ASP A 990 −9.673 −8.229 5.070 1.00 1.00 H ATOM 257 N TYR A 991 −9.296 −10.445 3.615 1.00 1.00 N ATOM 258 CA TYR A 991 −8.287 −11.480 3.236 1.00 1.00 C ATOM 259 C TYR A 991 −6.926 −10.954 2.710 1.00 1.00 C ATOM 260 O TYR A 991 −5.839 −11.105 3.245 1.00 1.00 O ATOM 261 CB TYR A 991 −8.950 −12.475 2.208 1.00 1.00 C ATOM 262 CG TYR A 991 −10.298 −12.880 2.832 1.00 1.00 C ATOM 263 CD1 TYR A 991 −10.351 −13.931 3.745 1.00 1.00 C ATOM 264 CD2 TYR A 991 −11.465 −12.205 2.437 1.00 1.00 C ATOM 265 CE1 TYR A 991 −11.595 −14.375 4.248 1.00 1.00 C ATOM 266 CE2 TYR A 991 −12.642 −12.571 3.062 1.00 1.00 C ATOM 267 CZ TYR A 991 −12.732 −13.582 4.034 1.00 1.00 C ATOM 268 OH TYR A 991 −13.907 −13.771 4.790 1.00 1.00 O ATOM 269 HA TYR A 991 −7.956 −12.077 4.124 1.00 1.00 H ATOM 270 HB2 TYR A 991 −8.335 −13.345 2.041 1.00 1.00 H ATOM 271 HB1 TYR A 991 −9.170 −12.024 1.253 1.00 1.00 H ATOM 272 HD2 TYR A 991 −11.470 −11.486 1.604 1.00 1.00 H ATOM 273 HE2 TYR A 991 −13.504 −11.980 2.760 1.00 1.00 H ATOM 274 HE1 TYR A 991 −11.699 −15.301 4.793 1.00 1.00 H ATOM 275 HD1 TYR A 991 −9.448 −14.408 4.025 1.00 1.00 H ATOM 276 HH TYR A 991 −13.778 −14.303 5.583 1.00 1.00 H ATOM 277 HN TYR A 991 −9.794 −10.612 4.496 1.00 1.00 H ATOM 278 N CYS A 992 −6.938 −10.246 1.549 1.00 1.00 N ATOM 279 CA CYS A 992 −5.661 −9.753 1.042 1.00 1.00 C ATOM 280 C CYS A 992 −5.042 −8.756 1.934 1.00 1.00 C ATOM 281 O CYS A 992 −3.817 −8.694 1.938 1.00 1.00 O ATOM 282 CB CYS A 992 −5.774 −9.219 −0.409 1.00 1.00 C ATOM 283 SG CYS A 992 −4.078 −8.786 −1.022 1.00 1.00 S ATOM 284 HA CYS A 992 −4.927 −10.570 0.998 1.00 1.00 H ATOM 285 HB1 CYS A 992 −6.423 −8.358 −0.502 1.00 1.00 H ATOM 286 HB2 CYS A 992 −6.183 −10.002 −1.123 1.00 1.00 H ATOM 287 H4 CYS A 992 −4.051 −7.962 −0.506 1.00 1.00 H ATOM 288 HN CYS A 992 −7.783 −10.051 1.063 1.00 1.00 H ATOM 289 N LEU A 993 −5.708 −7.900 2.699 1.00 1.00 N ATOM 290 CA LEU A 993 −4.931 −6.981 3.584 1.00 1.00 C ATOM 291 C LEU A 993 −4.006 −7.727 4.503 1.00 1.00 C ATOM 292 O LEU A 993 −2.983 −7.197 4.952 1.00 1.00 O ATOM 293 CB LEU A 993 −5.755 −5.795 4.079 1.00 1.00 C ATOM 294 CG LEU A 993 −6.872 −6.064 5.130 1.00 1.00 C ATOM 295 CD1 LEU A 993 −6.247 −6.740 6.375 1.00 1.00 C ATOM 296 CD2 LEU A 993 −7.701 −4.786 5.439 1.00 1.00 C ATOM 297 HA LEU A 993 −4.239 −6.443 2.929 1.00 1.00 H ATOM 298 HB1 LEU A 993 −6.247 −5.367 3.168 1.00 1.00 H ATOM 299 HB2 LEU A 993 −5.033 −5.063 4.537 1.00 1.00 H ATOM 300 HG LEU A 993 −7.475 −6.810 4.641 1.00 1.00 H ATOM 301 HD21 LEU A 993 −8.008 −4.367 4.484 1.00 1.00 H ATOM 302 HD22 LEU A 993 −7.104 −4.034 5.935 1.00 1.00 H ATOM 303 HD23 LEU A 993 −8.507 −5.069 6.022 1.00 1.00 H ATOM 304 HD11 LEU A 993 −5.894 −7.759 6.203 1.00 1.00 H ATOM 305 HD12 LEU A 993 −7.002 −6.762 7.187 1.00 1.00 H ATOM 306 HD13 LEU A 993 −5.412 −6.152 6.774 1.00 1.00 H ATOM 307 HN LEU A 993 −6.697 −7.968 2.796 1.00 1.00 H ATOM 308 N SER A 994 −4.399 −8.953 4.875 1.00 1.00 N ATOM 309 CA SER A 994 −3.499 −9.815 5.622 1.00 1.00 C ATOM 310 C SER A 994 −2.420 −10.265 4.652 1.00 1.00 C ATOM 311 O SER A 994 −1.250 −10.269 4.986 1.00 1.00 O ATOM 312 CB SER A 994 −4.271 −10.985 6.296 1.00 1.00 C ATOM 313 OG SER A 994 −3.331 −11.707 7.161 1.00 1.00 O ATOM 314 HA SER A 994 −3.102 −9.208 6.457 1.00 1.00 H ATOM 315 HB1 SER A 994 −4.675 −11.655 5.535 1.00 1.00 H ATOM 316 HB2 SER A 994 −5.075 −10.513 6.901 1.00 1.00 H ATOM 317 HG SER A 994 −3.713 −12.379 7.719 1.00 1.00 H ATOM 318 HN SER A 994 −5.256 −9.398 4.569 1.00 1.00 H ATOM 319 N HIE A 995 −2.775 −10.642 3.397 1.00 1.00 N ATOM 320 CA HIE A 995 −1.656 −10.790 2.414 1.00 1.00 C ATOM 321 C HIE A 995 −0.735 −9.562 2.453 1.00 1.00 C ATOM 322 O HIE A 995 0.465 −9.767 2.467 1.00 1.00 O ATOM 323 CB HIE A 995 −1.911 −11.029 0.873 1.00 1.00 C ATOM 324 CG HIE A 995 −2.366 −12.414 0.468 1.00 1.00 C ATOM 325 ND1 HIE A 995 −2.546 −12.824 −0.932 1.00 1.00 N ATOM 326 CD2 HIE A 995 −2.825 −13.476 1.162 1.00 1.00 C ATOM 327 CE1 HIE A 995 −2.989 −14.014 −0.959 1.00 1.00 C ATOM 328 NE2 HIE A 995 −3.171 −14.382 0.287 1.00 1.00 N ATOM 329 HA HIE A 995 −1.131 −11.692 2.792 1.00 1.00 H ATOM 330 HB1 HIE A 995 −2.554 −10.236 0.493 1.00 1.00 H ATOM 331 HB2 HIE A 995 −0.951 −11.012 0.413 1.00 1.00 H ATOM 332 HD2 HIE A 995 −2.954 −13.634 2.228 1.00 1.00 H ATOM 333 HE2 HIE A 995 −3.514 −15.315 0.582 1.00 1.00 H ATOM 334 HE1 HIE A 995 −3.176 −14.614 −1.833 1.00 1.00 H ATOM 335 HN HIE A 995 −3.757 −10.856 3.165 1.00 1.00 H ATOM 336 N ILE A 996 −1.238 −8.320 2.478 1.00 1.00 N ATOM 337 CA ILE A 996 −0.333 −7.197 2.482 1.00 1.00 C ATOM 338 C ILE A 996 0.493 −7.337 3.749 1.00 1.00 C ATOM 339 O ILE A 996 1.732 −7.170 3.672 1.00 1.00 O ATOM 340 CB ILE A 996 −1.046 −5.780 2.448 1.00 1.00 C ATOM 341 CG1 ILE A 996 −1.727 −5.590 1.063 1.00 1.00 C ATOM 342 CG2 ILE A 996 0.027 −4.664 2.711 1.00 1.00 C ATOM 343 CD1 ILE A 996 −2.657 −4.333 0.923 1.00 1.00 C ATOM 344 HA ILE A 996 0.390 −7.229 1.669 1.00 1.00 H ATOM 345 HB ILE A 996 −1.793 −5.805 3.293 1.00 1.00 H ATOM 346 HG11 ILE A 996 −2.387 −6.447 0.825 1.00 1.00 H ATOM 347 HG12 ILE A 996 −0.881 −5.474 0.385 1.00 1.00 H ATOM 348 HD11 ILE A 996 −3.465 −4.328 1.687 1.00 1.00 H ATOM 349 HD12 ILE A 996 −3.110 −4.393 −0.023 1.00 1.00 H ATOM 350 HD13 ILE A 996 −2.099 −3.413 0.981 1.00 1.00 H ATOM 351 HG21 ILE A 996 0.425 −4.816 3.711 1.00 1.00 H ATOM 352 HG22 ILE A 996 −0.426 −3.652 2.616 1.00 1.00 H ATOM 353 HG23 ILE A 996 0.807 −4.746 1.980 1.00 1.00 H ATOM 354 HN ILE A 996 −2.229 −8.105 2.534 1.00 1.00 H ATOM 355 N VAL A 997 −0.096 −7.589 4.917 1.00 1.00 N ATOM 356 CA VAL A 997 0.794 −7.743 6.053 1.00 1.00 C ATOM 357 C VAL A 997 1.783 −8.897 5.798 1.00 1.00 C ATOM 358 O VAL A 997 2.974 −8.626 5.799 1.00 1.00 O ATOM 359 CB VAL A 997 0.029 −7.900 7.429 1.00 1.00 C ATOM 360 CG1 VAL A 997 1.072 −8.097 8.607 1.00 1.00 C ATOM 361 CG2 VAL A 997 −0.763 −6.606 7.909 1.00 1.00 C ATOM 362 HA VAL A 997 1.363 −6.834 6.137 1.00 1.00 H ATOM 363 HB VAL A 997 −0.708 −8.675 7.338 1.00 1.00 H ATOM 364 HG11 VAL A 997 1.672 −9.091 8.459 1.00 1.00 H ATOM 365 HG12 VAL A 997 0.584 −8.105 9.574 1.00 1.00 H ATOM 366 HG13 VAL A 997 1.714 −7.278 8.694 1.00 1.00 H ATOM 367 HG21 VAL A 997 −0.238 −5.628 7.797 1.00 1.00 H ATOM 368 HG22 VAL A 997 −1.156 −6.668 8.928 1.00 1.00 H ATOM 369 HG23 VAL A 997 −1.621 −6.574 7.157 1.00 1.00 H ATOM 370 HN VAL A 997 −1.082 −7.731 5.024 1.00 1.00 H ATOM 371 N ASN A 998 1.272 −10.137 5.620 1.00 1.00 N ATOM 372 CA ASN A 998 2.188 −11.299 5.428 1.00 1.00 C ATOM 373 C ASN A 998 3.273 −10.974 4.449 1.00 1.00 C ATOM 374 O ASN A 998 4.451 −11.167 4.679 1.00 1.00 O ATOM 375 CB ASN A 998 1.367 −12.559 5.002 1.00 1.00 C ATOM 376 CG ASN A 998 2.231 −13.810 4.997 1.00 1.00 C ATOM 377 OD1 ASN A 998 2.670 −14.140 3.905 1.00 1.00 O ATOM 378 ND2 ASN A 998 2.467 −14.470 6.132 1.00 1.00 N ATOM 379 HA ASN A 998 2.616 −11.521 6.386 1.00 1.00 H ATOM 380 HB1 ASN A 998 0.891 −12.436 4.052 1.00 1.00 H ATOM 381 HB2 ASN A 998 0.514 −12.665 5.696 1.00 1.00 H ATOM 382 HD22 ASN A 998 2.897 −15.364 6.112 1.00 1.00 H ATOM 383 HD21 ASN A 998 2.312 −14.069 7.033 1.00 1.00 H ATOM 384 HN ASN A 998 0.313 −10.286 5.719 1.00 1.00 H ATOM 385 N LEU A 999 2.881 −10.391 3.316 1.00 1.00 N ATOM 386 CA LEU A 999 3.856 −9.988 2.322 1.00 1.00 C ATOM 387 C LEU A 999 4.903 −9.201 3.064 1.00 1.00 C ATOM 388 O LEU A 999 6.060 −9.601 3.015 1.00 1.00 O ATOM 389 CB LEU A 999 3.158 −9.272 1.177 1.00 1.00 C ATOM 390 CG LEU A 999 4.179 −8.528 0.215 1.00 1.00 C ATOM 391 CD1 LEU A 999 4.903 −9.527 −0.718 1.00 1.00 C ATOM 392 CD2 LEU A 999 3.464 −7.520 −0.646 1.00 1.00 C ATOM 393 HA LEU A 999 4.320 −10.935 1.944 1.00 1.00 H ATOM 394 HB1 LEU A 999 2.441 −8.548 1.532 1.00 1.00 H ATOM 395 HB2 LEU A 999 2.559 −10.037 0.608 1.00 1.00 H ATOM 396 HG LEU A 999 4.865 −7.916 0.821 1.00 1.00 H ATOM 397 HD21 LEU A 999 4.178 −7.005 −1.284 1.00 1.00 H ATOM 398 HD22 LEU A 999 2.997 −6.758 −0.017 1.00 1.00 H ATOM 399 HD23 LEU A 999 2.668 −7.932 −1.257 1.00 1.00 H ATOM 400 HD11 LEU A 999 4.130 −10.167 −1.186 1.00 1.00 H ATOM 401 HD12 LEU A 999 5.538 −10.184 −0.160 1.00 1.00 H ATOM 402 HD13 LEU A 999 5.521 −8.939 −1.445 1.00 1.00 H ATOM 403 HN LEU A 999 1.910 −10.254 3.145 1.00 1.00 H ATOM 404 N LEU A 1000 4.585 −8.059 3.731 1.00 1.00 N ATOM 405 CA LEU A 1000 5.596 −7.203 4.354 1.00 1.00 C ATOM 406 C LEU A 1000 6.383 −7.980 5.400 1.00 1.00 C ATOM 407 O LEU A 1000 7.598 −7.999 5.425 1.00 1.00 O ATOM 408 CB LEU A 1000 5.062 −5.871 5.014 1.00 1.00 C ATOM 409 CG LEU A 1000 4.991 −4.651 4.032 1.00 1.00 C ATOM 410 CD1 LEU A 1000 3.821 −4.842 3.112 1.00 1.00 C ATOM 411 CD2 LEU A 1000 4.850 −3.309 4.826 1.00 1.00 C ATOM 412 HA LEU A 1000 6.291 −6.869 3.564 1.00 1.00 H ATOM 413 HB1 LEU A 1000 5.764 −5.548 5.752 1.00 1.00 H ATOM 414 HB2 LEU A 1000 4.085 −6.045 5.513 1.00 1.00 H ATOM 415 HG LEU A 1000 5.902 −4.675 3.478 1.00 1.00 H ATOM 416 HD21 LEU A 1000 5.685 −3.136 5.555 1.00 1.00 H ATOM 417 HD22 LEU A 1000 3.875 −3.197 5.322 1.00 1.00 H ATOM 418 HD23 LEU A 1000 4.969 −2.550 4.059 1.00 1.00 H ATOM 419 HD11 LEU A 1000 3.817 −3.955 2.444 1.00 1.00 H ATOM 420 HD12 LEU A 1000 2.860 −4.843 3.696 1.00 1.00 H ATOM 421 HD13 LEU A 1000 3.881 −5.728 2.498 1.00 1.00 H ATOM 422 HN LEU A 1000 3.624 −7.798 3.854 1.00 1.00 H ATOM 423 N GLU A 1001 5.657 −8.475 6.433 1.00 1.00 N ATOM 424 CA GLU A 1001 6.268 −9.068 7.581 1.00 1.00 C ATOM 425 C GLU A 1001 6.909 −10.414 7.205 1.00 1.00 C ATOM 426 O GLU A 1001 8.065 −10.623 7.537 1.00 1.00 O ATOM 427 CB GLU A 1001 5.333 −9.253 8.748 1.00 1.00 C ATOM 428 CG GLU A 1001 4.709 −7.928 9.242 1.00 1.00 C ATOM 429 CD GLU A 1001 5.624 −6.853 9.748 1.00 1.00 C ATOM 430 OE1 GLU A 1001 5.510 −5.615 9.530 1.00 1.00 O ATOM 431 OE2 GLU A 1001 6.579 −7.191 10.502 1.00 1.00 O ATOM 432 HA GLU A 1001 7.154 −8.474 7.896 1.00 1.00 H ATOM 433 HB1 GLU A 1001 5.768 −9.714 9.702 1.00 1.00 H ATOM 434 HB2 GLU A 1001 4.420 −9.845 8.450 1.00 1.00 H ATOM 435 HG1 GLU A 1001 4.044 −8.152 10.121 1.00 1.00 H ATOM 436 HG2 GLU A 1001 4.147 −7.407 8.451 1.00 1.00 H ATOM 437 HN GLU A 1001 4.675 −8.541 6.420 1.00 1.00 H ATOM 438 N ASP A 1002 6.228 −11.349 6.578 1.00 1.00 N ATOM 439 CA ASP A 1002 6.803 −12.664 6.307 1.00 1.00 C ATOM 440 C ASP A 1002 7.640 −12.784 5.070 1.00 1.00 C ATOM 441 O ASP A 1002 8.690 −13.475 5.131 1.00 1.00 O ATOM 442 CB ASP A 1002 5.790 −13.787 6.372 1.00 1.00 C ATOM 443 CG ASP A 1002 5.207 −13.948 7.743 1.00 1.00 C ATOM 444 OD1 ASP A 1002 4.236 −13.227 8.054 1.00 1.00 O ATOM 445 OD2 ASP A 1002 5.770 −14.768 8.508 1.00 1.00 O ATOM 446 HA ASP A 1002 7.461 −12.913 7.107 1.00 1.00 H ATOM 447 HB1 ASP A 1002 6.336 −14.701 6.059 1.00 1.00 H ATOM 448 HB2 ASP A 1002 4.982 −13.617 5.641 1.00 1.00 H ATOM 449 HN ASP A 1002 5.301 −11.170 6.191 1.00 1.00 H ATOM 450 N TRP A 1003 7.309 −12.155 3.916 1.00 1.00 N ATOM 451 CA TRP A 1003 8.028 −12.521 2.712 1.00 1.00 C ATOM 452 C TRP A 1003 9.347 −11.717 2.607 1.00 1.00 C ATOM 453 O TRP A 1003 10.188 −12.008 1.776 1.00 1.00 O ATOM 454 CB TRP A 1003 7.245 −12.350 1.425 1.00 1.00 C ATOM 455 CG TRP A 1003 5.928 −13.105 1.426 1.00 1.00 C ATOM 456 CD1 TRP A 1003 5.234 −13.742 2.370 1.00 1.00 C ATOM 457 CD2 TRP A 1003 5.081 −13.269 0.214 1.00 1.00 C ATOM 458 NE1 TRP A 1003 4.125 −14.238 1.928 1.00 1.00 N ATOM 459 CE2 TRP A 1003 3.974 −13.995 0.622 1.00 1.00 C ATOM 460 CE3 TRP A 1003 5.245 −12.863 −1.108 1.00 1.00 C ATOM 461 CZ2 TRP A 1003 2.896 −14.356 −0.205 1.00 1.00 C ATOM 462 CZ3 TRP A 1003 4.207 −13.291 −1.962 1.00 1.00 C ATOM 463 CH2 TRP A 1003 3.067 −13.986 −1.528 1.00 1.00 C ATOM 464 HA TRP A 1003 8.356 −13.571 2.796 1.00 1.00 H ATOM 465 HB1 TRP A 1003 7.953 −12.648 0.620 1.00 1.00 H ATOM 466 HB2 TRP A 1003 7.032 −11.308 1.373 1.00 1.00 H ATOM 467 HE1 TRP A 1003 3.372 −14.672 2.522 1.00 1.00 H ATOM 468 HD1 TRP A 1003 5.553 −13.819 3.437 1.00 1.00 H ATOM 469 HZ2 TRP A 1003 2.034 −14.863 0.176 1.00 1.00 H ATOM 470 HH2 TRP A 1003 2.311 −14.188 −2.323 1.00 1.00 H ATOM 471 HZ3 TRP A 1003 4.220 −13.039 −3.034 1.00 1.00 H ATOM 472 HE3 TRP A 1003 6.091 −12.270 −1.397 1.00 1.00 H ATOM 473 HN TRP A 1003 6.524 −11.504 3.913 1.00 1.00 H ATOM 474 N GLY A 1004 9.574 −10.669 3.477 1.00 1.00 N ATOM 475 CA GLY A 1004 10.789 −9.895 3.350 1.00 1.00 C ATOM 476 C GLY A 1004 12.070 −10.653 2.944 1.00 1.00 C ATOM 477 O GLY A 1004 12.762 −10.229 2.015 1.00 1.00 O ATOM 478 HA2 GLY A 1004 11.108 −9.589 4.337 1.00 1.00 H ATOM 479 HA1 GLY A 1004 10.654 −9.048 2.670 1.00 1.00 H ATOM 480 HN GLY A 1004 8.925 −10.435 4.206 1.00 1.00 H ATOM 481 N PRO A 1005 12.579 −11.765 3.541 1.00 1.00 N ATOM 482 CA PRO A 1005 13.852 −12.345 3.150 1.00 1.00 C ATOM 483 C PRO A 1005 13.998 −12.666 1.707 1.00 1.00 C ATOM 484 O PRO A 1005 15.042 −12.420 1.155 1.00 1.00 O ATOM 485 CB PRO A 1005 13.861 −13.680 3.989 1.00 1.00 C ATOM 486 CG PRO A 1005 12.906 −13.370 5.191 1.00 1.00 C ATOM 487 CD PRO A 1005 11.799 −12.434 4.617 1.00 1.00 C ATOM 488 HA PRO A 1005 14.610 −11.606 3.479 1.00 1.00 H ATOM 489 HD2 PRO A 1005 11.403 −11.683 5.350 1.00 1.00 H ATOM 490 HD1 PRO A 1005 10.996 −13.058 4.147 1.00 1.00 H ATOM 491 HG2 PRO A 1005 13.524 −12.917 5.947 1.00 1.00 H ATOM 492 HG1 PRO A 1005 12.483 −14.261 5.628 1.00 1.00 H ATOM 493 HB1 PRO A 1005 14.879 −13.938 4.352 1.00 1.00 H ATOM 494 HB2 PRO A 1005 13.430 −14.571 3.445 1.00 1.00 H ATOM 495 N CYS A 1006 13.035 −13.296 1.074 1.00 1.00 N ATOM 496 CA CYS A 1006 13.140 −13.592 −0.390 1.00 1.00 C ATOM 497 C CYS A 1006 12.762 −12.375 −1.245 1.00 1.00 C ATOM 498 O CYS A 1006 13.351 −12.102 −2.280 1.00 1.00 O ATOM 499 CB CYS A 1006 12.201 −14.795 −0.743 1.00 1.00 C ATOM 500 SG CYS A 1006 12.536 −15.488 −2.352 1.00 1.00 S ATOM 501 HA CYS A 1006 14.177 −13.862 −0.671 1.00 1.00 H ATOM 502 HB1 CYS A 1006 11.120 −14.461 −0.654 1.00 1.00 H ATOM 503 HB2 CYS A 1006 12.290 −15.623 −0.005 1.00 1.00 H ATOM 504 HG CYS A 1006 12.338 −14.714 −2.962 1.00 1.00 H ATOM 505 HN CYS A 1006 12.202 −13.577 1.509 1.00 1.00 H ATOM 506 N ALA A 1007 11.768 −11.607 −0.809 1.00 1.00 N ATOM 507 CA ALA A 1007 11.279 −10.496 −1.619 1.00 1.00 C ATOM 508 C ALA A 1007 12.309 −9.452 −1.823 1.00 1.00 C ATOM 509 O ALA A 1007 12.480 −9.009 −2.932 1.00 1.00 O ATOM 510 CB ALA A 1007 9.999 −9.818 −1.009 1.00 1.00 C ATOM 511 HA ALA A 1007 11.063 −10.943 −2.589 1.00 1.00 H ATOM 512 HB1 ALA A 1007 9.218 −10.616 −0.823 1.00 1.00 H ATOM 513 HB2 ALA A 1007 9.534 −9.139 −1.712 1.00 1.00 H ATOM 514 HB3 ALA A 1007 10.199 −9.277 −0.051 1.00 1.00 H ATOM 515 HN ALA A 1007 11.257 −11.726 0.080 1.00 1.00 H ATOM 516 N GLU A 1008 13.008 −9.091 −0.725 1.00 1.00 N ATOM 517 CA GLU A 1008 13.693 −7.774 −0.696 1.00 1.00 C ATOM 518 C GLU A 1008 14.665 −7.691 0.450 1.00 1.00 C ATOM 519 O GLU A 1008 15.831 −7.723 0.199 1.00 1.00 O ATOM 520 CB GLU A 1008 12.634 −6.641 −0.630 1.00 1.00 C ATOM 521 CG GLU A 1008 13.185 −5.193 −0.873 1.00 1.00 C ATOM 522 CD GLU A 1008 12.086 −4.246 −1.424 1.00 1.00 C ATOM 523 OE1 GLU A 1008 12.389 −3.101 −1.843 1.00 1.00 O ATOM 524 OE2 GLU A 1008 10.882 −4.552 −1.441 1.00 1.00 O ATOM 525 HA GLU A 1008 14.197 −7.740 −1.668 1.00 1.00 H ATOM 526 HB1 GLU A 1008 12.101 −6.630 0.347 1.00 1.00 H ATOM 527 HB2 GLU A 1008 11.851 −6.902 −1.395 1.00 1.00 H ATOM 528 HG1 GLU A 1008 13.975 −5.220 −1.627 1.00 1.00 H ATOM 529 HG2 GLU A 1008 13.598 −4.707 0.027 1.00 1.00 H ATOM 530 HN GLU A 1008 12.900 −9.511 0.168 1.00 1.00 H ATOM 531 N HIS A 1009 14.191 −7.702 1.721 1.00 1.00 N ATOM 532 CA HIS A 1009 15.129 −7.834 2.854 1.00 1.00 C ATOM 533 C HIS A 1009 14.531 −8.513 4.111 1.00 1.00 C ATOM 534 O HIS A 1009 13.334 −8.355 4.185 1.00 1.00 O ATOM 535 CB HIS A 1009 15.698 −6.460 3.242 1.00 1.00 C ATOM 536 CG HIS A 1009 16.848 −6.553 4.172 1.00 1.00 C ATOM 537 ND1 HIS A 1009 17.993 −7.099 3.790 1.00 1.00 N ATOM 538 CD2 HIS A 1009 16.866 −6.123 5.466 1.00 1.00 C ATOM 539 CE1 HIS A 1009 18.802 −6.981 4.779 1.00 1.00 C ATOM 540 NE2 HIS A 1009 18.240 −6.420 5.737 1.00 1.00 N ATOM 541 HA HIS A 1009 15.965 −8.437 2.557 1.00 1.00 H ATOM 542 HB1 HIS A 1009 14.890 −5.845 3.691 1.00 1.00 H ATOM 543 HB2 HIS A 1009 15.993 −5.933 2.353 1.00 1.00 H ATOM 544 HD2 HIS A 1009 16.119 −5.622 6.058 1.00 1.00 H ATOM 545 HE1 HIS A 1009 19.819 −7.310 4.776 1.00 1.00 H ATOM 546 HD1 HIS A 1009 18.137 −7.520 2.864 1.00 1.00 H ATOM 547 HN HIS A 1009 13.219 −7.738 1.935 1.00 1.00 H ATOM 548 N GLY A 1010 15.273 −9.256 5.002 1.00 1.00 N ATOM 549 CA GLY A 1010 14.575 −10.077 5.994 1.00 1.00 C ATOM 550 C GLY A 1010 14.714 −9.643 7.436 1.00 1.00 C ATOM 551 O GLY A 1010 15.653 −10.008 8.103 1.00 1.00 O ATOM 552 HA2 GLY A 1010 14.989 −11.128 5.893 1.00 1.00 H ATOM 553 HA1 GLY A 1010 13.490 −10.283 5.842 1.00 1.00 H ATOM 554 HN GLY A 1010 16.306 −9.187 5.018 1.00 1.00 H ATOM 555 N GLU A 1011 13.728 −8.854 7.989 1.00 1.00 N ATOM 556 CA GLU A 1011 13.576 −8.614 9.409 1.00 1.00 C ATOM 557 C GLU A 1011 12.120 −8.382 9.661 1.00 1.00 C ATOM 558 O GLU A 1011 11.447 −7.923 8.762 1.00 1.00 O ATOM 559 CB GLU A 1011 14.497 −7.541 10.090 1.00 1.00 C ATOM 560 CG GLU A 1011 15.881 −7.338 9.382 1.00 1.00 C ATOM 561 CD GLU A 1011 16.599 −6.107 9.925 1.00 1.00 C ATOM 562 OE1 GLU A 1011 17.092 −6.200 11.097 1.00 1.00 O ATOM 563 OE2 GLU A 1011 16.641 −5.074 9.204 1.00 1.00 O ATOM 564 HA GLU A 1011 13.813 −9.563 9.869 1.00 1.00 H ATOM 565 HB1 GLU A 1011 14.790 −7.854 11.113 1.00 1.00 H ATOM 566 HB2 GLU A 1011 13.951 −6.587 10.133 1.00 1.00 H ATOM 567 HG1 GLU A 1011 15.735 −7.095 8.320 1.00 1.00 H ATOM 568 HG2 GLU A 1011 16.514 −8.204 9.420 1.00 1.00 H ATOM 569 HN GLU A 1011 13.020 −8.452 7.393 1.00 1.00 H ATOM 570 N HIS A 1012 11.609 −8.618 10.854 1.00 1.00 N ATOM 571 CA HIS A 1012 10.281 −8.224 11.285 1.00 1.00 C ATOM 572 C HIS A 1012 10.120 −6.697 11.403 1.00 1.00 C ATOM 573 O HIS A 1012 8.984 −6.206 11.289 1.00 1.00 O ATOM 574 CB HIS A 1012 10.009 −8.931 12.631 1.00 1.00 C ATOM 575 CG HIS A 1012 8.618 −8.870 13.196 1.00 1.00 C ATOM 576 ND1 HIS A 1012 7.532 −8.538 12.505 1.00 1.00 N ATOM 577 CD2 HIS A 1012 8.326 −9.177 14.481 1.00 1.00 C ATOM 578 CE1 HIS A 1012 6.524 −8.651 13.325 1.00 1.00 C ATOM 579 NE2 HIS A 1012 6.902 −9.013 14.449 1.00 1.00 N ATOM 580 HA HIS A 1012 9.522 −8.610 10.525 1.00 1.00 H ATOM 581 HB1 HIS A 1012 10.152 −9.977 12.534 1.00 1.00 H ATOM 582 HB2 HIS A 1012 10.717 −8.555 13.418 1.00 1.00 H ATOM 583 HD2 HIS A 1012 8.909 −9.453 15.354 1.00 1.00 H ATOM 584 HE1 HIS A 1012 5.463 −8.501 13.067 1.00 1.00 H ATOM 585 HD1 HIS A 1012 7.408 −8.258 11.514 1.00 1.00 H ATOM 586 HN HIS A 1012 12.300 −8.840 11.572 1.00 1.00 H ATOM 587 N HIS A 1013 11.232 −6.029 11.736 1.00 1.00 N ATOM 588 CA HIS A 1013 11.110 −4.544 11.780 1.00 1.00 C ATOM 589 C HIS A 1013 12.444 −4.134 11.211 1.00 1.00 C ATOM 590 O HIS A 1013 13.406 −4.740 11.670 1.00 1.00 O ATOM 591 CB HIS A 1013 10.910 −4.048 13.266 1.00 1.00 C ATOM 592 CG HIS A 1013 9.477 −4.364 13.626 1.00 1.00 C ATOM 593 ND1 HIS A 1013 9.121 −5.479 14.204 1.00 1.00 N ATOM 594 CD2 HIS A 1013 8.373 −3.633 13.366 1.00 1.00 C ATOM 595 CE1 HIS A 1013 7.838 −5.535 14.325 1.00 1.00 C ATOM 596 NE2 HIS A 1013 7.328 −4.511 13.833 1.00 1.00 N ATOM 597 HA HIS A 1013 10.262 −4.131 11.199 1.00 1.00 H ATOM 598 HB1 HIS A 1013 11.679 −4.363 13.999 1.00 1.00 H ATOM 599 HB2 HIS A 1013 10.996 −2.960 13.308 1.00 1.00 H ATOM 600 HD2 HIS A 1013 8.193 −2.661 12.879 1.00 1.00 H ATOM 601 HE1 HIS A 1013 7.261 −6.389 14.794 1.00 1.00 H ATOM 602 HD1 HIS A 1013 9.771 −6.235 14.500 1.00 1.00 H ATOM 603 HN HIS A 1013 12.195 −6.340 11.887 1.00 1.00 H ATOM 604 N ILE A 1014 12.590 −3.234 10.211 1.00 1.00 N ATOM 605 CA ILE A 1014 13.685 −3.372 9.255 1.00 1.00 C ATOM 606 C ILE A 1014 14.754 −2.275 9.212 1.00 1.00 C ATOM 607 O ILE A 1014 14.499 −1.144 9.624 1.00 1.00 O ATOM 608 CB ILE A 1014 13.171 −3.729 7.812 1.00 1.00 C ATOM 609 CG1 ILE A 1014 12.885 −5.239 7.605 1.00 1.00 C ATOM 610 CG2 ILE A 1014 13.960 −3.076 6.642 1.00 1.00 C ATOM 611 CD1 ILE A 1014 12.325 −5.628 6.248 1.00 1.00 C ATOM 612 HA ILE A 1014 14.282 −4.190 9.625 1.00 1.00 H ATOM 613 HB ILE A 1014 12.184 −3.275 7.657 1.00 1.00 H ATOM 614 HG11 ILE A 1014 12.319 −5.577 8.539 1.00 1.00 H ATOM 615 HG12 ILE A 1014 13.857 −5.787 7.696 1.00 1.00 H ATOM 616 HD11 ILE A 1014 11.944 −6.666 6.346 1.00 1.00 H ATOM 617 HD12 ILE A 1014 13.091 −5.524 5.442 1.00 1.00 H ATOM 618 HD13 ILE A 1014 11.464 −4.987 6.026 1.00 1.00 H ATOM 619 HG21 ILE A 1014 14.091 −1.994 6.867 1.00 1.00 H ATOM 620 HG22 ILE A 1014 13.499 −3.189 5.668 1.00 1.00 H ATOM 621 HG23 ILE A 1014 14.973 −3.496 6.609 1.00 1.00 H ATOM 622 HN ILE A 1014 11.903 −2.580 10.056 1.00 1.00 H ATOM 623 N ARG A 1015 16.014 −2.546 8.737 1.00 1.00 N ATOM 624 CA ARG A 1015 16.987 −1.486 8.662 1.00 1.00 C ATOM 625 C ARG A 1015 17.689 −1.508 7.323 1.00 1.00 C ATOM 626 O ARG A 1015 18.822 −1.972 7.278 1.00 1.00 O ATOM 627 CB ARG A 1015 18.007 −1.842 9.771 1.00 1.00 C ATOM 628 CG ARG A 1015 17.456 −1.744 11.238 1.00 1.00 C ATOM 629 CD ARG A 1015 18.060 −2.774 12.261 1.00 1.00 C ATOM 630 NE ARG A 1015 17.231 −3.975 12.319 1.00 1.00 N ATOM 631 CZ ARG A 1015 16.013 −4.069 12.839 1.00 1.00 C ATOM 632 NH1 ARG A 1015 15.292 −3.038 13.241 1.00 1.00 N ATOM 633 NH2 ARG A 1015 15.510 −5.259 12.831 1.00 1.00 N ATOM 634 HA ARG A 1015 16.611 −0.502 8.947 1.00 1.00 H ATOM 635 HB1 ARG A 1015 18.912 −1.220 9.712 1.00 1.00 H ATOM 636 HB2 ARG A 1015 18.351 −2.906 9.577 1.00 1.00 H ATOM 637 HG1 ARG A 1015 16.383 −1.931 11.217 1.00 1.00 H ATOM 638 HG2 ARG A 1015 17.609 −0.732 11.589 1.00 1.00 H ATOM 639 HD1 ARG A 1015 18.248 −2.319 13.240 1.00 1.00 H ATOM 640 HD2 ARG A 1015 19.070 −2.990 11.924 1.00 1.00 H ATOM 641 HE ARG A 1015 17.649 −4.860 11.908 1.00 1.00 H ATOM 642 HH12 ARG A 1015 14.286 −3.178 13.481 1.00 1.00 H ATOM 643 HH11 ARG A 1015 15.708 −2.115 13.328 1.00 1.00 H ATOM 644 HH22 ARG A 1015 14.536 −5.398 13.096 1.00 1.00 H ATOM 645 HH21 ARG A 1015 16.022 −6.088 12.521 1.00 1.00 H ATOM 646 HN ARG A 1015 16.256 −3.478 8.436 1.00 1.00 H ATOM 647 N ILE A 1016 17.112 −1.036 6.187 1.00 1.00 N ATOM 648 CA ILE A 1016 17.744 −1.151 4.861 1.00 1.00 C ATOM 649 C ILE A 1016 17.828 0.143 4.154 1.00 1.00 C ATOM 650 O ILE A 1016 17.215 0.456 3.143 1.00 1.00 O ATOM 651 CB ILE A 1016 16.852 −2.211 4.113 1.00 1.00 C ATOM 652 CG1 ILE A 1016 17.464 −2.750 2.756 1.00 1.00 C ATOM 653 CG2 ILE A 1016 15.409 −1.771 3.753 1.00 1.00 C ATOM 654 CD1 ILE A 1016 18.833 −3.425 2.918 1.00 1.00 C ATOM 655 HA ILE A 1016 18.749 −1.526 4.976 1.00 1.00 H ATOM 656 HB ILE A 1016 16.805 −3.106 4.737 1.00 1.00 H ATOM 657 HG11 ILE A 1016 17.570 −1.916 2.057 1.00 1.00 H ATOM 658 HG12 ILE A 1016 16.741 −3.458 2.341 1.00 1.00 H ATOM 659 HD11 ILE A 1016 19.274 −3.738 1.934 1.00 1.00 H ATOM 660 HD12 ILE A 1016 18.735 −4.359 3.455 1.00 1.00 H ATOM 661 HD13 ILE A 1016 19.573 −2.864 3.460 1.00 1.00 H ATOM 662 HG21 ILE A 1016 15.394 −1.127 2.833 1.00 1.00 H ATOM 663 HG22 ILE A 1016 14.863 −1.247 4.557 1.00 1.00 H ATOM 664 HG23 ILE A 1016 14.802 −2.654 3.541 1.00 1.00 H ATOM 665 HN ILE A 1016 16.227 −0.604 6.290 1.00 1.00 H ATOM 666 N PRO A 1017 18.621 1.174 4.671 1.00 1.00 N ATOM 667 CA PRO A 1017 19.242 1.116 5.940 1.00 1.00 C ATOM 668 C PRO A 1017 18.335 1.725 6.950 1.00 1.00 C ATOM 669 O PRO A 1017 17.226 1.983 6.608 1.00 1.00 O ATOM 670 CB PRO A 1017 20.375 2.093 5.695 1.00 1.00 C ATOM 671 CG PRO A 1017 19.695 3.181 4.807 1.00 1.00 C ATOM 672 CD PRO A 1017 18.792 2.397 3.813 1.00 1.00 C ATOM 673 HA PRO A 1017 19.600 0.156 6.335 1.00 1.00 H ATOM 674 HD2 PRO A 1017 19.329 2.199 2.845 1.00 1.00 H ATOM 675 HD1 PRO A 1017 17.866 2.928 3.603 1.00 1.00 H ATOM 676 HG2 PRO A 1017 20.511 3.776 4.321 1.00 1.00 H ATOM 677 HG1 PRO A 1017 19.030 3.841 5.449 1.00 1.00 H ATOM 678 HB1 PRO A 1017 21.116 1.507 5.158 1.00 1.00 H ATOM 679 HB2 PRO A 1017 20.922 2.417 6.574 1.00 1.00 H ATOM 680 N ARG A 1018 18.779 1.992 8.207 1.00 1.00 N ATOM 681 CA ARG A 1018 17.909 2.706 9.182 1.00 1.00 C ATOM 682 C ARG A 1018 17.542 4.047 8.616 1.00 1.00 C ATOM 683 O ARG A 1018 18.478 4.541 8.059 1.00 1.00 O ATOM 684 CB ARG A 1018 18.426 2.791 10.673 1.00 1.00 C ATOM 685 CG ARG A 1018 19.402 4.036 10.992 1.00 1.00 C ATOM 686 CD ARG A 1018 20.739 4.014 10.143 1.00 1.00 C ATOM 687 NE ARG A 1018 21.410 5.301 10.349 1.00 1.00 N ATOM 688 CZ ARG A 1018 21.016 6.405 9.756 1.00 1.00 C ATOM 689 NH1 ARG A 1018 20.049 6.477 8.903 1.00 1.00 N ATOM 690 NH2 ARG A 1018 21.604 7.529 10.073 1.00 1.00 N ATOM 691 HA ARG A 1018 17.009 2.059 9.180 1.00 1.00 H ATOM 692 HB1 ARG A 1018 18.926 1.763 10.841 1.00 1.00 H ATOM 693 HB2 ARG A 1018 17.567 2.860 11.362 1.00 1.00 H ATOM 694 HG1 ARG A 1018 19.608 3.965 12.092 1.00 1.00 H ATOM 695 HG2 ARG A 1018 18.800 4.907 10.742 1.00 1.00 H ATOM 696 HD1 ARG A 1018 20.683 3.797 9.046 1.00 1.00 H ATOM 697 HD2 ARG A 1018 21.308 3.163 10.562 1.00 1.00 H ATOM 698 HE ARG A 1018 22.227 5.305 11.015 1.00 1.00 H ATOM 699 HH12 ARG A 1018 19.677 7.409 8.592 1.00 1.00 H ATOM 700 HH11 ARG A 1018 19.563 5.660 8.503 1.00 1.00 H ATOM 701 HH22 ARG A 1018 21.435 8.443 9.626 1.00 1.00 H ATOM 702 HH21 ARG A 1018 22.377 7.548 10.756 1.00 1.00 H ATOM 703 HN ARG A 1018 19.689 1.690 8.504 1.00 1.00 H ATOM 704 N THR A 1019 16.342 4.646 8.771 1.00 1.00 N ATOM 705 CA THR A 1019 15.963 5.870 8.099 1.00 1.00 C ATOM 706 C THR A 1019 17.119 6.661 7.512 1.00 1.00 C ATOM 707 O THR A 1019 17.811 7.250 8.338 1.00 1.00 O ATOM 708 CB THR A 1019 15.176 6.800 9.031 1.00 1.00 C ATOM 709 OG1 THR A 1019 14.107 6.049 9.613 1.00 1.00 O ATOM 710 CG2 THR A 1019 14.667 8.092 8.334 1.00 1.00 C ATOM 711 HA THR A 1019 15.280 5.508 7.320 1.00 1.00 H ATOM 712 HB THR A 1019 15.827 7.064 9.924 1.00 1.00 H ATOM 713 HG1 THR A 1019 13.360 5.872 9.049 1.00 1.00 H ATOM 714 HG23 THR A 1019 14.028 8.640 9.037 1.00 1.00 H ATOM 715 HG21 THR A 1019 14.145 7.866 7.430 1.00 1.00 H ATOM 716 HG22 THR A 1019 15.487 8.755 8.092 1.00 1.00 H ATOM 717 HN THR A 1019 15.591 4.131 9.265 1.00 1.00 H ATOM 718 N PRO A 1020 17.430 6.731 6.176 1.00 1.00 N ATOM 719 CA PRO A 1020 18.658 7.406 5.722 1.00 1.00 C ATOM 720 C PRO A 1020 18.746 8.864 6.088 1.00 1.00 C ATOM 721 O PRO A 1020 19.810 9.296 6.487 1.00 1.00 O ATOM 722 CB PRO A 1020 18.650 7.085 4.198 1.00 1.00 C ATOM 723 CG PRO A 1020 17.161 6.890 3.860 1.00 1.00 C ATOM 724 CD PRO A 1020 16.646 6.138 5.141 1.00 1.00 C ATOM 725 HA PRO A 1020 19.511 6.905 6.196 1.00 1.00 H ATOM 726 HD2 PRO A 1020 16.893 5.028 5.160 1.00 1.00 H ATOM 727 HD1 PRO A 1020 15.618 6.310 5.250 1.00 1.00 H ATOM 728 HG2 PRO A 1020 17.012 6.380 2.894 1.00 1.00 H ATOM 729 HG1 PRO A 1020 16.726 7.913 3.768 1.00 1.00 H ATOM 730 HB1 PRO A 1020 19.107 6.093 4.090 1.00 1.00 H ATOM 731 HB2 PRO A 1020 19.185 7.823 3.554 1.00 1.00 H ATOM 732 N ALA A 1021 17.585 9.577 6.038 1.00 1.00 N ATOM 733 CA ALA A 1021 17.602 11.032 6.320 1.00 1.00 C ATOM 734 C ALA A 1021 16.275 11.586 5.848 1.00 1.00 C ATOM 735 O ALA A 1021 15.345 10.816 5.679 1.00 1.00 O ATOM 736 CB ALA A 1021 17.852 11.440 7.802 1.00 1.00 C ATOM 737 HA ALA A 1021 18.337 11.461 5.676 1.00 1.00 H ATOM 738 HB1 ALA A 1021 18.764 11.098 8.306 1.00 1.00 H ATOM 739 HB2 ALA A 1021 17.875 12.527 7.957 1.00 1.00 H ATOM 740 HB3 ALA A 1021 16.963 11.095 8.405 1.00 1.00 H ATOM 741 HN ALA A 1021 16.680 9.152 5.787 1.00 1.00 H ATOM 742 N ARG A 1022 16.120 12.927 5.722 1.00 1.00 N ATOM 743 CA ARG A 1022 14.899 13.481 5.135 1.00 1.00 C ATOM 744 C ARG A 1022 15.022 13.508 3.582 1.00 1.00 C ATOM 745 O ARG A 1022 15.120 14.546 2.933 1.00 1.00 O ATOM 746 CB ARG A 1022 14.518 14.956 5.579 1.00 1.00 C ATOM 747 CG ARG A 1022 14.320 15.063 7.122 1.00 1.00 C ATOM 748 CD ARG A 1022 13.430 14.008 7.799 1.00 1.00 C ATOM 749 NE ARG A 1022 13.016 14.505 9.134 1.00 1.00 N ATOM 750 CZ ARG A 1022 11.988 15.295 9.376 1.00 1.00 C ATOM 751 NH1 ARG A 1022 11.204 15.758 8.413 1.00 1.00 N ATOM 752 NH2 ARG A 1022 11.687 15.636 10.601 1.00 1.00 N ATOM 753 HA ARG A 1022 14.045 12.836 5.326 1.00 1.00 H ATOM 754 HB1 ARG A 1022 13.518 15.165 5.172 1.00 1.00 H ATOM 755 HB2 ARG A 1022 15.204 15.695 5.184 1.00 1.00 H ATOM 756 HG1 ARG A 1022 13.996 16.071 7.407 1.00 1.00 H ATOM 757 HG2 ARG A 1022 15.288 14.893 7.696 1.00 1.00 H ATOM 758 HD1 ARG A 1022 13.931 13.046 7.887 1.00 1.00 H ATOM 759 HD2 ARG A 1022 12.565 13.774 7.151 1.00 1.00 H ATOM 760 HE ARG A 1022 13.595 14.141 9.934 1.00 1.00 H ATOM 761 HH12 ARG A 1022 10.349 16.269 8.666 1.00 1.00 H ATOM 762 HH11 ARG A 1022 11.353 15.593 7.413 1.00 1.00 H ATOM 763 HH22 ARG A 1022 10.872 16.223 10.882 1.00 1.00 H ATOM 764 HH21 ARG A 1022 12.271 15.348 11.396 1.00 1.00 H ATOM 765 HN ARG A 1022 16.918 13.574 5.823 1.00 1.00 H ATOM 766 N VAL A 1023 15.073 12.283 3.012 1.00 1.00 N ATOM 767 CA VAL A 1023 15.273 12.074 1.597 1.00 1.00 C ATOM 768 C VAL A 1023 14.378 11.000 1.024 1.00 1.00 C ATOM 769 O VAL A 1023 14.774 10.330 0.099 1.00 1.00 O ATOM 770 CB VAL A 1023 16.753 11.699 1.206 1.00 1.00 C ATOM 771 CG1 VAL A 1023 17.637 12.969 1.434 1.00 1.00 C ATOM 772 CG2 VAL A 1023 17.181 10.477 2.104 1.00 1.00 C ATOM 773 HA VAL A 1023 14.944 12.951 0.998 1.00 1.00 H ATOM 774 HB VAL A 1023 16.778 11.494 0.137 1.00 1.00 H ATOM 775 HG11 VAL A 1023 18.673 12.806 1.007 1.00 1.00 H ATOM 776 HG12 VAL A 1023 17.701 13.246 2.486 1.00 1.00 H ATOM 777 HG13 VAL A 1023 17.170 13.814 0.863 1.00 1.00 H ATOM 778 HG21 VAL A 1023 17.212 10.724 3.138 1.00 1.00 H ATOM 779 HG22 VAL A 1023 16.430 9.661 2.006 1.00 1.00 H ATOM 780 HG23 VAL A 1023 18.136 10.112 1.690 1.00 1.00 H ATOM 781 HN VAL A 1023 15.004 11.454 3.568 1.00 1.00 H ATOM 782 N THR A 1024 13.160 10.779 1.573 1.00 1.00 N ATOM 783 CA THR A 1024 12.372 9.608 1.227 1.00 1.00 C ATOM 784 C THR A 1024 10.935 9.890 0.843 1.00 1.00 C ATOM 785 O THR A 1024 10.485 11.015 1.023 1.00 1.00 O ATOM 786 CB THR A 1024 12.275 8.696 2.522 1.00 1.00 C ATOM 787 OG1 THR A 1024 11.422 9.231 3.545 1.00 1.00 O ATOM 788 CG2 THR A 1024 13.640 8.367 3.107 1.00 1.00 C ATOM 789 HA THR A 1024 12.814 9.036 0.393 1.00 1.00 H ATOM 790 HB THR A 1024 11.791 7.804 2.224 1.00 1.00 H ATOM 791 HG1 THR A 1024 10.502 9.318 3.394 1.00 1.00 H ATOM 792 HG23 THR A 1024 14.197 7.868 2.298 1.00 1.00 H ATOM 793 HG21 THR A 1024 13.620 7.711 4.033 1.00 1.00 H ATOM 794 HG22 THR A 1024 14.198 9.266 3.335 1.00 1.00 H ATOM 795 HN THR A 1024 12.762 11.411 2.285 1.00 1.00 H ATOM 796 N GLY A 1025 10.185 8.874 0.351 1.00 1.00 N ATOM 797 CA GLY A 1025 8.734 8.969 0.398 1.00 1.00 C ATOM 798 C GLY A 1025 8.326 8.401 1.707 1.00 1.00 C ATOM 799 O GLY A 1025 9.232 8.218 2.517 1.00 1.00 O ATOM 800 HA2 GLY A 1025 8.166 8.441 −0.345 1.00 1.00 H ATOM 801 HA1 GLY A 1025 8.350 9.977 0.410 1.00 1.00 H ATOM 802 HN GLY A 1025 10.598 7.974 0.035 1.00 1.00 H ATOM 803 N GLY A 1026 7.008 8.082 1.999 1.00 1.00 N ATOM 804 CA GLY A 1026 6.791 7.393 3.295 1.00 1.00 C ATOM 805 C GLY A 1026 5.418 7.637 3.830 1.00 1.00 C ATOM 806 O GLY A 1026 4.888 8.695 3.496 1.00 1.00 O ATOM 807 HA2 GLY A 1026 7.488 7.734 4.077 1.00 1.00 H ATOM 808 HA1 GLY A 1026 6.929 6.286 3.267 1.00 1.00 H ATOM 809 HN GLY A 1026 6.294 8.212 1.295 1.00 1.00 H ATOM 810 N VAL A 1027 4.808 6.665 4.575 1.00 1.00 N ATOM 811 CA VAL A 1027 3.346 6.644 4.858 1.00 1.00 C ATOM 812 C VAL A 1027 2.999 5.915 6.098 1.00 1.00 C ATOM 813 O VAL A 1027 3.709 5.029 6.544 1.00 1.00 O ATOM 814 CB VAL A 1027 2.616 5.960 3.638 1.00 1.00 C ATOM 815 CG1 VAL A 1027 2.652 6.832 2.344 1.00 1.00 C ATOM 816 CG2 VAL A 1027 3.035 4.473 3.448 1.00 1.00 C ATOM 817 HA VAL A 1027 2.950 7.672 5.004 1.00 1.00 H ATOM 818 HB VAL A 1027 1.564 5.966 3.870 1.00 1.00 H ATOM 819 HG11 VAL A 1027 2.444 7.827 2.695 1.00 1.00 H ATOM 820 HG12 VAL A 1027 3.639 6.684 1.874 1.00 1.00 H ATOM 821 HG13 VAL A 1027 1.869 6.467 1.624 1.00 1.00 H ATOM 822 HG21 VAL A 1027 2.938 3.815 4.333 1.00 1.00 H ATOM 823 HG22 VAL A 1027 2.391 4.065 2.645 1.00 1.00 H ATOM 824 HG23 VAL A 1027 4.106 4.372 3.104 1.00 1.00 H ATOM 825 HN VAL A 1027 5.273 5.810 4.784 1.00 1.00 H ATOM 826 N PHE A 1028 1.894 6.323 6.764 1.00 1.00 N ATOM 827 CA PHE A 1028 1.539 5.707 8.037 1.00 1.00 C ATOM 828 C PHE A 1028 0.328 4.864 7.801 1.00 1.00 C ATOM 829 O PHE A 1028 −0.753 5.340 8.145 1.00 1.00 O ATOM 830 CB PHE A 1028 1.276 6.894 9.064 1.00 1.00 C ATOM 831 CG PHE A 1028 1.037 6.511 10.563 1.00 1.00 C ATOM 832 CD1 PHE A 1028 2.061 5.823 11.222 1.00 1.00 C ATOM 833 CD2 PHE A 1028 −0.124 6.875 11.317 1.00 1.00 C ATOM 834 CE1 PHE A 1028 2.015 5.498 12.579 1.00 1.00 C ATOM 835 CE2 PHE A 1028 −0.111 6.607 12.703 1.00 1.00 C ATOM 836 CZ PHE A 1028 0.928 5.939 13.328 1.00 1.00 C ATOM 837 HA PHE A 1028 2.444 5.182 8.477 1.00 1.00 H ATOM 838 HB1 PHE A 1028 0.372 7.381 8.624 1.00 1.00 H ATOM 839 HB2 PHE A 1028 2.185 7.529 9.043 1.00 1.00 H ATOM 840 HD2 PHE A 1028 −0.929 7.394 10.815 1.00 1.00 H ATOM 841 HE2 PHE A 1028 −0.997 6.943 13.184 1.00 1.00 H ATOM 842 HZ PHE A 1028 0.926 5.716 14.364 1.00 1.00 H ATOM 843 HE1 PHE A 1028 2.791 4.888 13.051 1.00 1.00 H ATOM 844 HD1 PHE A 1028 2.943 5.531 10.685 1.00 1.00 H ATOM 845 HN PHE A 1028 1.329 7.077 6.348 1.00 1.00 H ATOM 846 N LEU A 1029 0.445 3.661 7.177 1.00 1.00 N ATOM 847 CA LEU A 1029 −0.702 2.765 6.963 1.00 1.00 C ATOM 848 C LEU A 1029 −1.381 2.346 8.273 1.00 1.00 C ATOM 849 O LEU A 1029 −1.312 1.170 8.574 1.00 1.00 O ATOM 850 CB LEU A 1029 −0.449 1.530 6.073 1.00 1.00 C ATOM 851 CG LEU A 1029 0.262 1.770 4.709 1.00 1.00 C ATOM 852 CD1 LEU A 1029 0.664 0.451 3.952 1.00 1.00 C ATOM 853 CD2 LEU A 1029 −0.588 2.712 3.750 1.00 1.00 C ATOM 854 HA LEU A 1029 −1.428 3.398 6.420 1.00 1.00 H ATOM 855 HB1 LEU A 1029 −1.401 1.013 5.841 1.00 1.00 H ATOM 856 HB2 LEU A 1029 0.222 0.889 6.653 1.00 1.00 H ATOM 857 HG LEU A 1029 1.229 2.324 4.865 1.00 1.00 H ATOM 858 HD21 LEU A 1029 −0.643 3.703 4.237 1.00 1.00 H ATOM 859 HD22 LEU A 1029 −0.225 2.784 2.729 1.00 1.00 H ATOM 860 HD23 LEU A 1029 −1.598 2.299 3.653 1.00 1.00 H ATOM 861 HD11 LEU A 1029 −0.162 −0.245 3.883 1.00 1.00 H ATOM 862 HD12 LEU A 1029 1.173 0.568 3.018 1.00 1.00 H ATOM 863 HD13 LEU A 1029 1.338 −0.090 4.611 1.00 1.00 H ATOM 864 HN LEU A 1029 1.352 3.346 6.923 1.00 1.00 H ATOM 865 N VAL A 1030 −2.036 3.276 9.017 1.00 1.00 N ATOM 866 CA VAL A 1030 −2.514 2.944 10.363 1.00 1.00 C ATOM 867 C VAL A 1030 −3.928 3.493 10.529 1.00 1.00 C ATOM 868 O VAL A 1030 −4.092 4.628 10.930 1.00 1.00 O ATOM 869 CB VAL A 1030 −1.541 3.514 11.483 1.00 1.00 C ATOM 870 CG1 VAL A 1030 −2.162 3.124 12.889 1.00 1.00 C ATOM 871 CG2 VAL A 1030 −0.087 2.979 11.373 1.00 1.00 C ATOM 872 HA VAL A 1030 −2.540 1.855 10.563 1.00 1.00 H ATOM 873 HB VAL A 1030 −1.548 4.632 11.413 1.00 1.00 H ATOM 874 HG11 VAL A 1030 −2.219 2.041 12.943 1.00 1.00 H ATOM 875 HG12 VAL A 1030 −1.504 3.425 13.753 1.00 1.00 H ATOM 876 HG13 VAL A 1030 −3.156 3.534 13.088 1.00 1.00 H ATOM 877 HG21 VAL A 1030 −0.039 1.865 11.449 1.00 1.00 H ATOM 878 HG22 VAL A 1030 0.249 3.224 10.390 1.00 1.00 H ATOM 879 HG23 VAL A 1030 0.566 3.487 12.175 1.00 1.00 H ATOM 880 HN VAL A 1030 −2.069 4.237 8.753 1.00 1.00 H ATOM 881 N ASP A 1031 −4.998 2.703 10.264 1.00 1.00 N ATOM 882 CA ASP A 1031 −6.323 3.075 10.705 1.00 1.00 C ATOM 883 C ASP A 1031 −6.418 2.597 12.147 1.00 1.00 C ATOM 884 O ASP A 1031 −6.875 1.501 12.395 1.00 1.00 O ATOM 885 CB ASP A 1031 −7.488 2.651 9.759 1.00 1.00 C ATOM 886 CG ASP A 1031 −8.840 2.958 10.310 1.00 1.00 C ATOM 887 OD1 ASP A 1031 −9.102 4.085 10.803 1.00 1.00 O ATOM 888 OD2 ASP A 1031 −9.828 2.098 10.213 1.00 1.00 O ATOM 889 HA ASP A 1031 −6.432 4.192 10.719 1.00 1.00 H ATOM 890 HB1 ASP A 1031 −7.353 1.578 9.643 1.00 1.00 H ATOM 891 HB2 ASP A 1031 −7.464 3.159 8.758 1.00 1.00 H ATOM 892 HN ASP A 1031 −4.859 1.753 9.898 1.00 1.00 H ATOM 893 N LYS A 1032 −5.862 3.344 13.110 1.00 1.00 N ATOM 894 CA LYS A 1032 −5.706 2.950 14.510 1.00 1.00 C ATOM 895 C LYS A 1032 −4.925 1.647 14.580 1.00 1.00 C ATOM 896 O LYS A 1032 −4.731 1.017 13.557 1.00 1.00 O ATOM 897 CB LYS A 1032 −7.091 2.783 15.277 1.00 1.00 C ATOM 898 CG LYS A 1032 −8.139 3.950 15.213 1.00 1.00 C ATOM 899 CD LYS A 1032 −8.936 4.138 13.871 1.00 1.00 C ATOM 900 CE LYS A 1032 −9.780 2.937 13.357 1.00 1.00 C ATOM 901 NZ LYS A 1032 −10.757 3.340 12.246 1.00 1.00 N ATOM 902 HA LYS A 1032 −5.080 3.744 14.990 1.00 1.00 H ATOM 903 HB1 LYS A 1032 −6.811 2.664 16.340 1.00 1.00 H ATOM 904 HB2 LYS A 1032 −7.618 1.874 14.876 1.00 1.00 H ATOM 905 HG1 LYS A 1032 −8.961 3.749 15.941 1.00 1.00 H ATOM 906 HG2 LYS A 1032 −7.649 4.846 15.626 1.00 1.00 H ATOM 907 HD1 LYS A 1032 −8.175 4.437 13.137 1.00 1.00 H ATOM 908 HD2 LYS A 1032 −9.655 4.947 13.949 1.00 1.00 H ATOM 909 HE1 LYS A 1032 −9.035 2.196 13.035 1.00 1.00 H ATOM 910 HE2 LYS A 1032 −10.376 2.455 14.189 1.00 1.00 H ATOM 911 HZ1 LYS A 1032 −11.791 3.366 12.555 1.00 1.00 H ATOM 912 HZ2 LYS A 1032 −10.523 4.239 11.643 1.00 1.00 H ATOM 913 HZ3 LYS A 1032 −10.702 2.515 11.579 1.00 1.00 H ATOM 914 HN LYS A 1032 −5.520 4.269 12.905 1.00 1.00 H ATOM 915 N ASN A 1033 −4.474 1.146 15.742 1.00 1.00 N ATOM 916 CA ASN A 1033 −4.194 −0.297 15.887 1.00 1.00 C ATOM 917 C ASN A 1033 −3.293 −0.801 14.799 1.00 1.00 C ATOM 918 O ASN A 1033 −3.750 −1.617 14.000 1.00 1.00 O ATOM 919 CB ASN A 1033 −5.670 −0.883 15.792 1.00 1.00 C ATOM 920 CG ASN A 1033 −6.578 −0.353 16.832 1.00 1.00 C ATOM 921 OD1 ASN A 1033 −6.164 0.418 17.676 1.00 1.00 O ATOM 922 ND2 ASN A 1033 −7.878 −0.744 16.760 1.00 1.00 N ATOM 923 HA ASN A 1033 −3.714 −0.569 16.839 1.00 1.00 H ATOM 924 HB1 ASN A 1033 −5.611 −1.978 15.909 1.00 1.00 H ATOM 925 HB2 ASN A 1033 −6.092 −0.589 14.786 1.00 1.00 H ATOM 926 HD22 ASN A 1033 −8.577 −0.360 17.383 1.00 1.00 H ATOM 927 HD21 ASN A 1033 −8.205 −1.419 16.074 1.00 1.00 H ATOM 928 HN ASN A 1033 −4.525 1.717 16.563 1.00 1.00 H ATOM 929 N PRO A 1034 −2.009 −0.374 14.637 1.00 1.00 N ATOM 930 CA PRO A 1034 −1.185 −0.979 13.653 1.00 1.00 C ATOM 931 C PRO A 1034 −1.365 −2.449 13.617 1.00 1.00 C ATOM 932 O PRO A 1034 −1.454 −3.054 12.573 1.00 1.00 O ATOM 933 CB PRO A 1034 0.269 −0.630 14.070 1.00 1.00 C ATOM 934 CG PRO A 1034 0.067 0.748 14.701 1.00 1.00 C ATOM 935 CD PRO A 1034 −1.283 0.562 15.468 1.00 1.00 C ATOM 936 HA PRO A 1034 −1.446 −0.588 12.622 1.00 1.00 H ATOM 937 HD2 PRO A 1034 −1.836 1.442 15.716 1.00 1.00 H ATOM 938 HD1 PRO A 1034 −1.096 0.033 16.401 1.00 1.00 H ATOM 939 HG2 PRO A 1034 0.017 1.617 14.013 1.00 1.00 H ATOM 940 HG1 PRO A 1034 0.846 0.962 15.467 1.00 1.00 H ATOM 941 HB1 PRO A 1034 0.580 −1.357 14.802 1.00 1.00 H ATOM 942 HB2 PRO A 1034 0.947 −0.601 13.175 1.00 1.00 H ATOM 943 N HIE A 1035 −1.359 −3.141 14.808 1.00 1.00 N ATOM 944 CA HIE A 1035 −1.317 −4.643 14.797 1.00 1.00 C ATOM 945 C HIE A 1035 −1.640 −5.112 16.190 1.00 1.00 C ATOM 946 O HIE A 1035 −0.673 −5.423 16.834 1.00 1.00 O ATOM 947 CB HIE A 1035 0.039 −5.159 14.265 1.00 1.00 C ATOM 948 H HIE A 1035 −1.281 −2.744 15.686 1.00 1.00 H ATOM 949 CG HIE A 1035 0.354 −6.621 14.446 1.00 1.00 C ATOM 950 ND1 HIE A 1035 1.578 −7.286 14.207 1.00 1.00 N ATOM 951 CD2 HIE A 1035 −0.421 −7.629 14.836 1.00 1.00 C ATOM 952 HA HIE A 1035 −2.089 −4.989 14.115 1.00 1.00 H ATOM 953 CE1 HIE A 1035 1.478 −8.515 14.463 1.00 1.00 C ATOM 954 NE2 HIE A 1035 0.253 −8.771 14.850 1.00 1.00 N ATOM 955 HB2 HIE A 1035 0.855 −4.624 14.759 1.00 1.00 H ATOM 956 HB1 HIE A 1035 0.171 −4.956 13.222 1.00 1.00 H ATOM 957 HD2 HIE A 1035 −1.480 −7.468 15.037 1.00 1.00 H ATOM 958 HE1 HIE A 1035 2.355 −9.189 14.363 1.00 1.00 H ATOM 959 HE2 HIE A 1035 −0.085 −9.690 15.150 1.00 1.00 H ATOM 960 N ASN A 1036 −2.910 −5.164 16.691 1.00 1.00 N ATOM 961 CA ASN A 1036 −4.136 −4.875 15.844 1.00 1.00 C ATOM 962 C ASN A 1036 −5.263 −4.472 16.807 1.00 1.00 C ATOM 963 O ASN A 1036 −4.970 −4.084 17.923 1.00 1.00 O ATOM 964 CB ASN A 1036 −4.482 −6.073 14.903 1.00 1.00 C ATOM 965 CG ASN A 1036 −5.157 −7.102 15.763 1.00 1.00 C ATOM 966 OD1 ASN A 1036 −6.376 −7.257 15.743 1.00 1.00 O ATOM 967 ND2 ASN A 1036 −4.383 −7.913 16.523 1.00 1.00 N ATOM 968 HA ASN A 1036 −3.959 −3.937 15.251 1.00 1.00 H ATOM 969 HB1 ASN A 1036 −5.130 −5.788 14.061 1.00 1.00 H ATOM 970 HB2 ASN A 1036 −3.638 −6.561 14.445 1.00 1.00 H ATOM 971 HD22 ASN A 1036 −4.686 −8.580 17.131 1.00 1.00 H ATOM 972 HD21 ASN A 1036 −3.359 −7.811 16.535 1.00 1.00 H ATOM 973 HN ASN A 1036 −3.071 −5.409 17.685 1.00 1.00 H ATOM 974 N THR A 1037 −6.594 −4.481 16.470 1.00 1.00 N ATOM 975 CA THR A 1037 −7.700 −4.097 17.389 1.00 1.00 C ATOM 976 C THR A 1037 −8.906 −3.861 16.522 1.00 1.00 C ATOM 977 O THR A 1037 −8.830 −4.381 15.418 1.00 1.00 O ATOM 978 CB THR A 1037 −8.207 −5.234 18.307 1.00 1.00 C ATOM 979 OG1 THR A 1037 −9.321 −4.854 19.141 1.00 1.00 O ATOM 980 CG2 THR A 1037 −7.094 −6.008 19.023 1.00 1.00 C ATOM 981 HA THR A 1037 −7.503 −3.154 17.938 1.00 1.00 H ATOM 982 HB THR A 1037 −8.637 −5.986 17.627 1.00 1.00 H ATOM 983 HG1 THR A 1037 −9.069 −4.190 19.780 1.00 1.00 H ATOM 984 HG23 THR A 1037 −6.300 −6.368 18.382 1.00 1.00 H ATOM 985 HG21 THR A 1037 −6.691 −5.266 19.751 1.00 1.00 H ATOM 986 HG22 THR A 1037 −7.509 −6.875 19.581 1.00 1.00 H ATOM 987 HN THR A 1037 −6.787 −4.808 15.557 1.00 1.00 H ATOM 988 N ALA A 1038 −10.036 −3.185 16.947 1.00 1.00 N ATOM 989 CA ALA A 1038 −11.086 −2.839 15.998 1.00 1.00 C ATOM 990 C ALA A 1038 −10.459 −2.406 14.685 1.00 1.00 C ATOM 991 O ALA A 1038 −9.377 −1.845 14.612 1.00 1.00 O ATOM 992 CB ALA A 1038 −11.861 −1.612 16.556 1.00 1.00 C ATOM 993 HA ALA A 1038 −11.736 −3.734 15.885 1.00 1.00 H ATOM 994 HB1 ALA A 1038 −12.177 −1.626 17.600 1.00 1.00 H ATOM 995 HB2 ALA A 1038 −11.219 −0.703 16.440 1.00 1.00 H ATOM 996 HB3 ALA A 1038 −12.749 −1.455 15.917 1.00 1.00 H ATOM 997 HN ALA A 1038 −10.095 −2.929 17.911 1.00 1.00 H ATOM 998 N GLU A 1039 −11.224 −2.588 13.565 1.00 1.00 N ATOM 999 CA GLU A 1039 −10.831 −2.038 12.277 1.00 1.00 C ATOM 1000 C GLU A 1039 −9.411 −2.435 11.839 1.00 1.00 C ATOM 1001 O GLU A 1039 −9.227 −3.381 11.052 1.00 1.00 O ATOM 1002 CB GLU A 1039 −11.140 −0.513 12.279 1.00 1.00 C ATOM 1003 CG GLU A 1039 −12.659 −0.175 12.381 1.00 1.00 C ATOM 1004 CD GLU A 1039 −12.885 1.303 12.189 1.00 1.00 C ATOM 1005 OE1 GLU A 1039 −13.310 1.823 11.153 1.00 1.00 O ATOM 1006 OE2 GLU A 1039 −12.543 2.080 13.130 1.00 1.00 O ATOM 1007 HA GLU A 1039 −11.423 −2.499 11.439 1.00 1.00 H ATOM 1008 HB1 GLU A 1039 −10.629 −0.012 13.114 1.00 1.00 H ATOM 1009 HB2 GLU A 1039 −10.771 −0.052 11.363 1.00 1.00 H ATOM 1010 HG1 GLU A 1039 −13.223 −0.735 11.639 1.00 1.00 H ATOM 1011 HG2 GLU A 1039 −13.019 −0.610 13.320 1.00 1.00 H ATOM 1012 HN GLU A 1039 −12.061 −3.035 13.569 1.00 1.00 H ATOM 1013 N SER A 1040 −8.357 −1.708 12.312 1.00 1.00 N ATOM 1014 CA SER A 1040 −6.977 −1.982 11.941 1.00 1.00 C ATOM 1015 C SER A 1040 −6.681 −2.124 10.466 1.00 1.00 C ATOM 1016 O SER A 1040 −5.829 −2.905 10.090 1.00 1.00 O ATOM 1017 CB SER A 1040 −6.419 −3.111 12.810 1.00 1.00 C ATOM 1018 OG SER A 1040 −5.037 −3.364 12.715 1.00 1.00 O ATOM 1019 HA SER A 1040 −6.446 −1.084 12.216 1.00 1.00 H ATOM 1020 HB1 SER A 1040 −6.614 −2.873 13.943 1.00 1.00 H ATOM 1021 HB2 SER A 1040 −6.964 −4.023 12.499 1.00 1.00 H ATOM 1022 HG SER A 1040 −4.445 −2.709 13.147 1.00 1.00 H ATOM 1023 HN SER A 1040 −8.537 −1.063 13.105 1.00 1.00 H ATOM 1024 N ARG A 1041 −7.449 −1.317 9.683 1.00 1.00 N ATOM 1025 CA ARG A 1041 −7.344 −1.379 8.197 1.00 1.00 C ATOM 1026 C ARG A 1041 −6.081 −0.713 7.740 1.00 1.00 C ATOM 1027 O ARG A 1041 −5.471 0.037 8.471 1.00 1.00 O ATOM 1028 CB ARG A 1041 −8.527 −0.722 7.490 1.00 1.00 C ATOM 1029 CG ARG A 1041 −9.942 −1.108 8.029 1.00 1.00 C ATOM 1030 CD ARG A 1041 −11.066 −0.380 7.217 1.00 1.00 C ATOM 1031 NE ARG A 1041 −12.403 −0.426 7.806 1.00 1.00 N ATOM 1032 CZ ARG A 1041 −12.755 0.418 8.744 1.00 1.00 C ATOM 1033 NH1 ARG A 1041 −11.904 1.343 9.199 1.00 1.00 N ATOM 1034 NH2 ARG A 1041 −13.937 0.325 9.230 1.00 1.00 N ATOM 1035 HA ARG A 1041 −7.315 −2.450 7.932 1.00 1.00 H ATOM 1036 HB1 ARG A 1041 −8.509 −0.934 6.402 1.00 1.00 H ATOM 1037 HB2 ARG A 1041 −8.408 0.409 7.586 1.00 1.00 H ATOM 1038 HG1 ARG A 1041 −10.051 −2.205 7.988 1.00 1.00 H ATOM 1039 HG2 ARG A 1041 −10.154 −0.862 9.062 1.00 1.00 H ATOM 1040 HD1 ARG A 1041 −10.773 0.615 6.893 1.00 1.00 H ATOM 1041 HD2 ARG A 1041 −11.056 −0.916 6.279 1.00 1.00 H ATOM 1042 HE ARG A 1041 −13.080 −1.113 7.407 1.00 1.00 H ATOM 1043 HH12 ARG A 1041 −12.254 2.068 9.852 1.00 1.00 H ATOM 1044 HH11 ARG A 1041 −10.914 1.440 8.906 1.00 1.00 H ATOM 1045 HH22 ARG A 1041 −14.263 0.873 10.029 1.00 1.00 H ATOM 1046 HH21 ARG A 1041 −14.566 −0.421 8.938 1.00 1.00 H ATOM 1047 HN ARG A 1041 −8.034 −0.634 10.099 1.00 1.00 H ATOM 1048 N LEU A 1042 −5.644 −0.940 6.496 1.00 1.00 N ATOM 1049 CA LEU A 1042 −4.437 −0.250 6.004 1.00 1.00 C ATOM 1050 C LEU A 1042 −4.772 0.948 5.114 1.00 1.00 C ATOM 1051 O LEU A 1042 −4.245 1.048 4.016 1.00 1.00 O ATOM 1052 CB LEU A 1042 −3.450 −1.244 5.274 1.00 1.00 C ATOM 1053 CG LEU A 1042 −2.920 −2.438 6.131 1.00 1.00 C ATOM 1054 CD1 LEU A 1042 −2.109 −3.503 5.362 1.00 1.00 C ATOM 1055 CD2 LEU A 1042 −2.109 −1.928 7.332 1.00 1.00 C ATOM 1056 HA LEU A 1042 −3.841 0.258 6.808 1.00 1.00 H ATOM 1057 HB1 LEU A 1042 −2.642 −0.709 4.798 1.00 1.00 H ATOM 1058 HB2 LEU A 1042 −3.974 −1.734 4.410 1.00 1.00 H ATOM 1059 HG LEU A 1042 −3.819 −2.970 6.512 1.00 1.00 H ATOM 1060 HD21 LEU A 1042 −1.264 −1.324 6.978 1.00 1.00 H ATOM 1061 HD22 LEU A 1042 −2.778 −1.402 8.005 1.00 1.00 H ATOM 1062 HD23 LEU A 1042 −1.653 −2.747 7.930 1.00 1.00 H ATOM 1063 HD11 LEU A 1042 −1.124 −3.131 5.000 1.00 1.00 H ATOM 1064 HD12 LEU A 1042 −1.984 −4.386 5.976 1.00 1.00 H ATOM 1065 HD13 LEU A 1042 −2.701 −3.803 4.456 1.00 1.00 H ATOM 1066 HN LEU A 1042 −6.182 −1.548 5.926 1.00 1.00 H ATOM 1067 N VAL A 1043 −5.622 1.878 5.608 1.00 1.00 N ATOM 1068 CA VAL A 1043 −5.925 3.100 4.855 1.00 1.00 C ATOM 1069 C VAL A 1043 −4.654 3.832 4.401 1.00 1.00 C ATOM 1070 O VAL A 1043 −3.668 3.689 5.109 1.00 1.00 O ATOM 1071 CB VAL A 1043 −6.798 4.024 5.754 1.00 1.00 C ATOM 1072 CG1 VAL A 1043 −6.899 5.517 5.284 1.00 1.00 C ATOM 1073 CG2 VAL A 1043 −8.248 3.510 5.912 1.00 1.00 C ATOM 1074 HA VAL A 1043 −6.428 2.818 3.926 1.00 1.00 H ATOM 1075 HB VAL A 1043 −6.293 4.023 6.722 1.00 1.00 H ATOM 1076 HG11 VAL A 1043 −7.585 6.222 5.814 1.00 1.00 H ATOM 1077 HG12 VAL A 1043 −5.907 6.013 5.180 1.00 1.00 H ATOM 1078 HG13 VAL A 1043 −7.330 5.470 4.276 1.00 1.00 H ATOM 1079 HG21 VAL A 1043 −8.198 2.473 6.227 1.00 1.00 H ATOM 1080 HG22 VAL A 1043 −8.908 4.087 6.550 1.00 1.00 H ATOM 1081 HG23 VAL A 1043 −8.753 3.528 4.917 1.00 1.00 H ATOM 1082 HN VAL A 1043 −5.960 1.714 6.581 1.00 1.00 H ATOM 1083 N VAL A 1044 −4.728 4.588 3.267 1.00 1.00 N ATOM 1084 CA VAL A 1044 −3.533 5.277 2.772 1.00 1.00 C ATOM 1085 C VAL A 1044 −3.361 6.662 3.317 1.00 1.00 C ATOM 1086 O VAL A 1044 −4.313 7.272 3.794 1.00 1.00 O ATOM 1087 CB VAL A 1044 −3.459 5.217 1.194 1.00 1.00 C ATOM 1088 CG1 VAL A 1044 −3.450 3.743 0.684 1.00 1.00 C ATOM 1089 CG2 VAL A 1044 −4.599 5.943 0.449 1.00 1.00 C ATOM 1090 HA VAL A 1044 −2.667 4.756 3.209 1.00 1.00 H ATOM 1091 HB VAL A 1044 −2.441 5.641 0.958 1.00 1.00 H ATOM 1092 HG11 VAL A 1044 −2.639 3.243 1.145 1.00 1.00 H ATOM 1093 HG12 VAL A 1044 −4.341 3.202 0.917 1.00 1.00 H ATOM 1094 HG13 VAL A 1044 −3.321 3.707 −0.385 1.00 1.00 H ATOM 1095 HG21 VAL A 1044 −5.592 5.595 0.774 1.00 1.00 H ATOM 1096 HG22 VAL A 1044 −4.560 7.010 0.734 1.00 1.00 H ATOM 1097 HG23 VAL A 1044 −4.492 5.940 −0.650 1.00 1.00 H ATOM 1098 HN VAL A 1044 −5.572 4.547 2.719 1.00 1.00 H ATOM 1099 N ASP A 1045 −2.147 7.261 3.179 1.00 1.00 N ATOM 1100 CA ASP A 1045 −1.771 8.466 3.930 1.00 1.00 C ATOM 1101 C ASP A 1045 −0.577 9.153 3.248 1.00 1.00 C ATOM 1102 O ASP A 1045 0.118 8.532 2.457 1.00 1.00 O ATOM 1103 CB ASP A 1045 −1.359 8.087 5.397 1.00 1.00 C ATOM 1104 CG ASP A 1045 −0.359 9.011 6.002 1.00 1.00 C ATOM 1105 OD1 ASP A 1045 −0.791 10.160 6.177 1.00 1.00 O ATOM 1106 OD2 ASP A 1045 0.833 8.664 6.245 1.00 1.00 O ATOM 1107 HA ASP A 1045 −2.611 9.127 3.881 1.00 1.00 H ATOM 1108 HB1 ASP A 1045 −1.007 7.031 5.455 1.00 1.00 H ATOM 1109 HB2 ASP A 1045 −2.337 8.086 5.941 1.00 1.00 H ATOM 1110 HN ASP A 1045 −1.392 6.783 2.693 1.00 1.00 H ATOM 1111 N PHE A 1046 −0.285 10.477 3.475 1.00 1.00 N ATOM 1112 CA PHE A 1046 0.702 11.240 2.701 1.00 1.00 C ATOM 1113 C PHE A 1046 1.779 11.679 3.708 1.00 1.00 C ATOM 1114 O PHE A 1046 2.402 12.695 3.395 1.00 1.00 O ATOM 1115 CB PHE A 1046 0.015 12.428 1.940 1.00 1.00 C ATOM 1116 CG PHE A 1046 −0.522 13.524 2.908 1.00 1.00 C ATOM 1117 CD1 PHE A 1046 0.278 14.639 3.196 1.00 1.00 C ATOM 1118 CD2 PHE A 1046 −1.858 13.517 3.415 1.00 1.00 C ATOM 1119 CE1 PHE A 1046 −0.266 15.704 3.875 1.00 1.00 C ATOM 1120 CE2 PHE A 1046 −2.295 14.490 4.293 1.00 1.00 C ATOM 1121 CZ PHE A 1046 −1.488 15.585 4.510 1.00 1.00 C ATOM 1122 HA PHE A 1046 1.236 10.624 1.971 1.00 1.00 H ATOM 1123 HB1 PHE A 1046 −0.849 12.006 1.374 1.00 1.00 H ATOM 1124 HB2 PHE A 1046 0.709 12.757 1.175 1.00 1.00 H ATOM 1125 HD2 PHE A 1046 −2.543 12.760 3.092 1.00 1.00 H ATOM 1126 HE2 PHE A 1046 −3.268 14.364 4.698 1.00 1.00 H ATOM 1127 HZ PHE A 1046 −1.752 16.372 5.182 1.00 1.00 H ATOM 1128 HE1 PHE A 1046 0.212 16.635 3.901 1.00 1.00 H ATOM 1129 HD1 PHE A 1046 1.293 14.720 2.845 1.00 1.00 H ATOM 1130 HN PHE A 1046 −0.722 10.950 4.239 1.00 1.00 H ATOM 1131 N SER A 1047 2.025 10.996 4.826 1.00 1.00 N ATOM 1132 CA SER A 1047 3.022 11.568 5.779 1.00 1.00 C ATOM 1133 C SER A 1047 4.402 11.289 5.276 1.00 1.00 C ATOM 1134 O SER A 1047 5.112 10.463 5.855 1.00 1.00 O ATOM 1135 CB SER A 1047 2.825 11.065 7.224 1.00 1.00 C ATOM 1136 OG SER A 1047 2.994 9.639 7.422 1.00 1.00 O ATOM 1137 HA SER A 1047 2.972 12.680 5.777 1.00 1.00 H ATOM 1138 HB1 SER A 1047 1.831 11.312 7.609 1.00 1.00 H ATOM 1139 HB2 SER A 1047 3.539 11.572 7.866 1.00 1.00 H ATOM 1140 HG SER A 1047 2.322 9.069 7.012 1.00 1.00 H ATOM 1141 HN SER A 1047 1.605 10.091 4.965 1.00 1.00 H ATOM 1142 N GLN A 1048 4.898 11.972 4.199 1.00 1.00 N ATOM 1143 CA GLN A 1048 6.253 11.656 3.667 1.00 1.00 C ATOM 1144 C GLN A 1048 7.307 12.423 4.446 1.00 1.00 C ATOM 1145 O GLN A 1048 8.039 13.250 3.878 1.00 1.00 O ATOM 1146 CB GLN A 1048 6.391 11.985 2.163 1.00 1.00 C ATOM 1147 CG GLN A 1048 5.338 11.340 1.266 1.00 1.00 C ATOM 1148 CD GLN A 1048 5.696 11.402 −0.239 1.00 1.00 C ATOM 1149 OE1 GLN A 1048 6.250 10.404 −0.712 1.00 1.00 O ATOM 1150 NE2 GLN A 1048 5.530 12.540 −0.923 1.00 1.00 N ATOM 1151 HA GLN A 1048 6.455 10.566 3.762 1.00 1.00 H ATOM 1152 HB1 GLN A 1048 7.427 11.638 1.936 1.00 1.00 H ATOM 1153 HB2 GLN A 1048 6.356 13.056 1.891 1.00 1.00 H ATOM 1154 HG1 GLN A 1048 5.139 10.288 1.534 1.00 1.00 H ATOM 1155 HG2 GLN A 1048 4.373 11.860 1.444 1.00 1.00 H ATOM 1156 HE22 GLN A 1048 5.754 12.520 −1.892 1.00 1.00 H ATOM 1157 HE21 GLN A 1048 5.062 13.299 −0.492 1.00 1.00 H ATOM 1158 HN GLN A 1048 4.322 12.678 3.757 1.00 1.00 H ATOM 1159 N PHE A 1049 7.448 12.195 5.760 1.00 1.00 N ATOM 1160 CA PHE A 1049 8.498 12.912 6.571 1.00 1.00 C ATOM 1161 C PHE A 1049 8.601 14.403 6.232 1.00 1.00 C ATOM 1162 O PHE A 1049 7.665 15.130 6.512 1.00 1.00 O ATOM 1163 CB PHE A 1049 9.801 12.078 6.511 1.00 1.00 C ATOM 1164 CG PHE A 1049 9.473 10.773 7.198 1.00 1.00 C ATOM 1165 CD1 PHE A 1049 9.854 10.496 8.519 1.00 1.00 C ATOM 1166 CD2 PHE A 1049 8.902 9.694 6.495 1.00 1.00 C ATOM 1167 CE1 PHE A 1049 9.626 9.285 9.188 1.00 1.00 C ATOM 1168 CE2 PHE A 1049 8.482 8.542 7.201 1.00 1.00 C ATOM 1169 CZ PHE A 1049 8.811 8.358 8.545 1.00 1.00 C ATOM 1170 HA PHE A 1049 8.198 12.971 7.638 1.00 1.00 H ATOM 1171 HB1 PHE A 1049 10.563 12.551 7.155 1.00 1.00 H ATOM 1172 HB2 PHE A 1049 10.132 11.975 5.445 1.00 1.00 H ATOM 1173 HD2 PHE A 1049 8.738 9.638 5.419 1.00 1.00 H ATOM 1174 HE2 PHE A 1049 7.941 7.798 6.654 1.00 1.00 H ATOM 1175 HZ PHE A 1049 8.432 7.522 9.132 1.00 1.00 H ATOM 1176 HE1 PHE A 1049 10.105 9.034 10.133 1.00 1.00 H ATOM 1177 HD1 PHE A 1049 10.439 11.238 9.063 1.00 1.00 H ATOM 1178 HN PHE A 1049 6.838 11.539 6.215 1.00 1.00 H ATOM 1179 N SER A 1050 9.677 14.898 5.553 1.00 1.00 N ATOM 1180 CA SER A 1050 9.657 16.301 5.183 1.00 1.00 C ATOM 1181 C SER A 1050 8.806 16.291 3.968 1.00 1.00 C ATOM 1182 O SER A 1050 9.248 16.495 2.835 1.00 1.00 O ATOM 1183 CB SER A 1050 11.091 16.966 4.968 1.00 1.00 C ATOM 1184 OG SER A 1050 11.822 17.056 6.204 1.00 1.00 O ATOM 1185 HA SER A 1050 9.134 16.968 5.888 1.00 1.00 H ATOM 1186 HB1 SER A 1050 11.585 16.339 4.248 1.00 1.00 H ATOM 1187 HB2 SER A 1050 11.028 18.029 4.549 1.00 1.00 H ATOM 1188 HG SER A 1050 11.416 17.706 6.822 1.00 1.00 H ATOM 1189 HN SER A 1050 10.417 14.348 5.200 1.00 1.00 H ATOM 1190 N ARG A 1051 7.504 16.069 4.104 1.00 1.00 N ATOM 1191 CA ARG A 1051 6.512 16.140 3.037 1.00 1.00 C ATOM 1192 C ARG A 1051 6.472 17.509 2.374 1.00 1.00 C ATOM 1193 O ARG A 1051 6.785 18.476 3.011 1.00 1.00 O ATOM 1194 CB ARG A 1051 5.120 15.778 3.598 1.00 1.00 C ATOM 1195 CG ARG A 1051 4.306 16.806 4.460 1.00 1.00 C ATOM 1196 CD ARG A 1051 4.940 17.278 5.811 1.00 1.00 C ATOM 1197 NE ARG A 1051 6.076 18.199 5.698 1.00 1.00 N ATOM 1198 CZ ARG A 1051 6.823 18.520 6.683 1.00 1.00 C ATOM 1199 NH1 ARG A 1051 6.585 18.076 7.890 1.00 1.00 N ATOM 1200 NH2 ARG A 1051 7.854 19.308 6.424 1.00 1.00 N ATOM 1201 HA ARG A 1051 6.832 15.389 2.281 1.00 1.00 H ATOM 1202 HB1 ARG A 1051 4.471 15.533 2.718 1.00 1.00 H ATOM 1203 HB2 ARG A 1051 5.249 14.823 4.155 1.00 1.00 H ATOM 1204 HG1 ARG A 1051 4.005 17.775 3.978 1.00 1.00 H ATOM 1205 HG2 ARG A 1051 3.346 16.301 4.662 1.00 1.00 H ATOM 1206 HD1 ARG A 1051 4.146 17.821 6.416 1.00 1.00 H ATOM 1207 HD2 ARG A 1051 5.223 16.302 6.247 1.00 1.00 H ATOM 1208 HE ARG A 1051 6.253 18.609 4.683 1.00 1.00 H ATOM 1209 HH12 ARG A 1051 7.259 18.162 8.677 1.00 1.00 H ATOM 1210 HH11 ARG A 1051 5.682 17.702 8.148 1.00 1.00 H ATOM 1211 HH22 ARG A 1051 8.490 19.556 7.201 1.00 1.00 H ATOM 1212 HH21 ARG A 1051 8.113 19.593 5.446 1.00 1.00 H ATOM 1213 HN ARG A 1051 7.091 15.980 5.023 1.00 1.00 H ATOM 1214 N GLY A 1052 6.144 17.610 1.076 1.00 1.00 N ATOM 1215 CA GLY A 1052 6.082 18.919 0.416 1.00 1.00 C ATOM 1216 C GLY A 1052 6.344 18.699 −1.076 1.00 1.00 C ATOM 1217 O GLY A 1052 7.496 18.626 −1.468 1.00 1.00 O ATOM 1218 HA2 GLY A 1052 6.806 19.612 0.837 1.00 1.00 H ATOM 1219 HA1 GLY A 1052 5.124 19.350 0.569 1.00 1.00 H ATOM 1220 HN GLY A 1052 5.846 16.823 0.506 1.00 1.00 H ATOM 1221 N ASN A 1053 5.319 18.634 −1.957 1.00 1.00 N ATOM 1222 CA ASN A 1053 5.571 18.512 −3.401 1.00 1.00 C ATOM 1223 C ASN A 1053 5.958 17.059 −3.749 1.00 1.00 C ATOM 1224 O ASN A 1053 5.080 16.261 −3.510 1.00 1.00 O ATOM 1225 CB ASN A 1053 6.435 19.666 −3.989 1.00 1.00 C ATOM 1226 CG ASN A 1053 6.220 19.804 −5.457 1.00 1.00 C ATOM 1227 OD1 ASN A 1053 7.032 19.326 −6.235 1.00 1.00 O ATOM 1228 ND2 ASN A 1053 5.086 20.449 −5.832 1.00 1.00 N ATOM 1229 HA ASN A 1053 4.610 18.552 −3.953 1.00 1.00 H ATOM 1230 HB1 ASN A 1053 6.204 20.551 −3.410 1.00 1.00 H ATOM 1231 HB2 ASN A 1053 7.529 19.499 −3.827 1.00 1.00 H ATOM 1232 HD22 ASN A 1053 4.824 20.564 −6.801 1.00 1.00 H ATOM 1233 HD21 ASN A 1053 4.556 20.789 −5.135 1.00 1.00 H ATOM 1234 HN ASN A 1053 4.314 18.623 −1.676 1.00 1.00 H ATOM 1235 N TYR A 1054 7.115 16.707 −4.319 1.00 1.00 N ATOM 1236 CA TYR A 1054 7.490 15.320 −4.492 1.00 1.00 C ATOM 1237 C TYR A 1054 8.413 14.937 −5.648 1.00 1.00 C ATOM 1238 O TYR A 1054 8.056 14.155 −6.504 1.00 1.00 O ATOM 1239 CB TYR A 1054 7.946 14.703 −3.110 1.00 1.00 C ATOM 1240 CG TYR A 1054 8.415 13.228 −3.148 1.00 1.00 C ATOM 1241 CD1 TYR A 1054 7.971 12.304 −4.079 1.00 1.00 C ATOM 1242 CD2 TYR A 1054 9.339 12.840 −2.178 1.00 1.00 C ATOM 1243 CE1 TYR A 1054 8.430 11.001 −4.054 1.00 1.00 C ATOM 1244 CE2 TYR A 1054 9.883 11.563 −2.224 1.00 1.00 C ATOM 1245 CZ TYR A 1054 9.480 10.613 −3.186 1.00 1.00 C ATOM 1246 OH TYR A 1054 10.162 9.431 −3.347 1.00 1.00 O ATOM 1247 HA TYR A 1054 6.591 14.758 −4.725 1.00 1.00 H ATOM 1248 HB2 TYR A 1054 8.807 15.291 −2.736 1.00 1.00 H ATOM 1249 HB1 TYR A 1054 7.162 14.845 −2.378 1.00 1.00 H ATOM 1250 HD2 TYR A 1054 9.517 13.532 −1.381 1.00 1.00 H ATOM 1251 HE2 TYR A 1054 10.632 11.272 −1.505 1.00 1.00 H ATOM 1252 HE1 TYR A 1054 8.050 10.266 −4.751 1.00 1.00 H ATOM 1253 HD1 TYR A 1054 7.259 12.641 −4.834 1.00 1.00 H ATOM 1254 HH TYR A 1054 10.018 8.870 −2.588 1.00 1.00 H ATOM 1255 HN TYR A 1054 7.851 17.300 −4.544 1.00 1.00 H ATOM 1256 N ARG A 1055 9.656 15.467 −5.703 1.00 1.00 N ATOM 1257 CA ARG A 1055 10.519 15.062 −6.778 1.00 1.00 C ATOM 1258 C ARG A 1055 9.965 15.381 −8.133 1.00 1.00 C ATOM 1259 O ARG A 1055 10.227 14.601 −9.036 1.00 1.00 O ATOM 1260 CB ARG A 1055 10.921 13.576 −6.733 1.00 1.00 C ATOM 1261 CG ARG A 1055 11.537 13.150 −5.337 1.00 1.00 C ATOM 1262 CD ARG A 1055 11.715 11.599 −5.245 1.00 1.00 C ATOM 1263 NE ARG A 1055 12.681 10.992 −6.145 1.00 1.00 N ATOM 1264 CZ ARG A 1055 12.890 9.687 −6.214 1.00 1.00 C ATOM 1265 NH1 ARG A 1055 12.252 8.780 −5.489 1.00 1.00 N ATOM 1266 NH2 ARG A 1055 13.798 9.351 −7.104 1.00 1.00 N ATOM 1267 HA ARG A 1055 11.388 15.676 −6.840 1.00 1.00 H ATOM 1268 HB1 ARG A 1055 10.057 12.926 −6.897 1.00 1.00 H ATOM 1269 HB2 ARG A 1055 11.634 13.380 −7.558 1.00 1.00 H ATOM 1270 HG1 ARG A 1055 12.508 13.712 −5.108 1.00 1.00 H ATOM 1271 HG2 ARG A 1055 10.849 13.428 −4.516 1.00 1.00 H ATOM 1272 HD1 ARG A 1055 12.053 11.359 −4.190 1.00 1.00 H ATOM 1273 HD2 ARG A 1055 10.754 11.135 −5.390 1.00 1.00 H ATOM 1274 HE ARG A 1055 13.173 11.645 −6.742 1.00 1.00 H ATOM 1275 HH12 ARG A 1055 12.593 7.800 −5.568 1.00 1.00 H ATOM 1276 HH11 ARG A 1055 11.615 9.066 −4.733 1.00 1.00 H ATOM 1277 HH22 ARG A 1055 14.051 8.360 −7.286 1.00 1.00 H ATOM 1278 HH21 ARG A 1055 14.306 10.056 −7.659 1.00 1.00 H ATOM 1279 HN ARG A 1055 9.988 16.103 −4.991 1.00 1.00 H ATOM 1280 N VAL A 1056 9.202 16.473 −8.359 1.00 1.00 N ATOM 1281 CA VAL A 1056 8.770 16.893 −9.686 1.00 1.00 C ATOM 1282 C VAL A 1056 8.505 18.362 −9.888 1.00 1.00 C ATOM 1283 O VAL A 1056 9.185 18.953 −10.711 1.00 1.00 O ATOM 1284 CB VAL A 1056 7.455 16.112 −10.084 1.00 1.00 C ATOM 1285 CG1 VAL A 1056 7.066 16.502 −11.548 1.00 1.00 C ATOM 1286 CG2 VAL A 1056 7.591 14.558 −10.032 1.00 1.00 C ATOM 1287 HA VAL A 1056 9.540 16.579 −10.373 1.00 1.00 H ATOM 1288 HB VAL A 1056 6.585 16.301 −9.460 1.00 1.00 H ATOM 1289 HG11 VAL A 1056 7.876 16.385 −12.281 1.00 1.00 H ATOM 1290 HG12 VAL A 1056 6.742 17.534 −11.588 1.00 1.00 H ATOM 1291 HG13 VAL A 1056 6.203 15.836 −11.843 1.00 1.00 H ATOM 1292 HG21 VAL A 1056 8.332 14.223 −10.798 1.00 1.00 H ATOM 1293 HG22 VAL A 1056 7.835 14.250 −9.060 1.00 1.00 H ATOM 1294 HG23 VAL A 1056 6.625 14.067 −10.181 1.00 1.00 H ATOM 1295 HN VAL A 1056 8.993 17.132 −7.618 1.00 1.00 H ATOM 1296 N SER A 1057 7.509 18.936 −9.155 1.00 1.00 N ATOM 1297 CA SER A 1057 6.985 20.332 −9.409 1.00 1.00 C ATOM 1298 C SER A 1057 5.496 20.339 −9.523 1.00 1.00 C ATOM 1299 O SER A 1057 4.763 20.349 −8.522 1.00 1.00 O ATOM 1300 CB SER A 1057 7.699 21.255 −10.463 1.00 1.00 C ATOM 1301 OG SER A 1057 7.564 20.901 −11.794 1.00 1.00 O ATOM 1302 HA SER A 1057 7.208 20.805 −8.416 1.00 1.00 H ATOM 1303 HB1 SER A 1057 7.205 22.198 −10.334 1.00 1.00 H ATOM 1304 HB2 SER A 1057 8.761 21.405 −10.238 1.00 1.00 H ATOM 1305 HG SER A 1057 7.996 20.093 −12.041 1.00 1.00 H ATOM 1306 HN SER A 1057 7.120 18.415 −8.346 1.00 1.00 H ATOM 1307 N TRP A 1058 4.870 20.373 −10.727 1.00 1.00 N ATOM 1308 CA TRP A 1058 3.445 20.509 −10.895 1.00 1.00 C ATOM 1309 C TRP A 1058 3.058 19.984 −12.235 1.00 1.00 C ATOM 1310 O TRP A 1058 2.866 20.800 −13.120 1.00 1.00 O ATOM 1311 CB TRP A 1058 3.179 22.028 −10.784 1.00 1.00 C ATOM 1312 CG TRP A 1058 3.665 22.687 −9.506 1.00 1.00 C ATOM 1313 CD1 TRP A 1058 4.699 23.599 −9.341 1.00 1.00 C ATOM 1314 CD2 TRP A 1058 3.147 22.472 −8.117 1.00 1.00 C ATOM 1315 NE1 TRP A 1058 4.850 23.909 −8.074 1.00 1.00 N ATOM 1316 CE2 TRP A 1058 3.922 23.285 −7.329 1.00 1.00 C ATOM 1317 CE3 TRP A 1058 2.161 21.666 −7.574 1.00 1.00 C ATOM 1318 CZ2 TRP A 1058 3.753 23.389 −5.945 1.00 1.00 C ATOM 1319 CZ3 TRP A 1058 1.987 21.671 −6.191 1.00 1.00 C ATOM 1320 CH2 TRP A 1058 2.718 22.613 −5.396 1.00 1.00 C ATOM 1321 HA TRP A 1058 2.925 19.952 −10.114 1.00 1.00 H ATOM 1322 HB1 TRP A 1058 3.696 22.603 −11.620 1.00 1.00 H ATOM 1323 HB2 TRP A 1058 2.095 22.175 −10.851 1.00 1.00 H ATOM 1324 HE1 TRP A 1058 5.553 24.563 −7.694 1.00 1.00 H ATOM 1325 HD1 TRP A 1058 5.344 24.056 −10.071 1.00 1.00 H ATOM 1326 HZ2 TRP A 1058 4.426 24.029 −5.359 1.00 1.00 H ATOM 1327 HH2 TRP A 1058 2.452 22.706 −4.338 1.00 1.00 H ATOM 1328 HZ3 TRP A 1058 1.313 21.006 −5.640 1.00 1.00 H ATOM 1329 HE3 TRP A 1058 1.544 21.113 −8.208 1.00 1.00 H ATOM 1330 HN TRP A 1058 5.490 20.361 −11.529 1.00 1.00 H ATOM 1331 N PRO A 1059 2.987 18.624 −12.476 1.00 1.00 N ATOM 1332 CA PRO A 1059 2.786 18.260 −13.879 1.00 1.00 C ATOM 1333 C PRO A 1059 1.323 18.384 −14.144 1.00 1.00 C ATOM 1334 O PRO A 1059 0.689 17.360 −13.918 1.00 1.00 O ATOM 1335 CB PRO A 1059 3.350 16.847 −13.882 1.00 1.00 C ATOM 1336 CG PRO A 1059 3.076 16.423 −12.412 1.00 1.00 C ATOM 1337 CD PRO A 1059 3.206 17.612 −11.479 1.00 1.00 C ATOM 1338 HA PRO A 1059 3.333 18.922 −14.560 1.00 1.00 H ATOM 1339 HD2 PRO A 1059 2.414 17.616 −10.700 1.00 1.00 H ATOM 1340 HD1 PRO A 1059 4.194 17.753 −11.053 1.00 1.00 H ATOM 1341 HG2 PRO A 1059 3.788 15.709 −12.129 1.00 1.00 H ATOM 1342 HG1 PRO A 1059 2.074 15.963 −12.318 1.00 1.00 H ATOM 1343 HB1 PRO A 1059 2.920 16.164 −14.655 1.00 1.00 H ATOM 1344 HB2 PRO A 1059 4.451 16.917 −14.010 1.00 1.00 H ATOM 1345 N LYS A 1060 0.768 19.588 −14.556 1.00 1.00 N ATOM 1346 CA LYS A 1060 −0.669 19.695 −14.694 1.00 1.00 C ATOM 1347 C LYS A 1060 −1.179 19.888 −16.101 1.00 1.00 C ATOM 1348 O LYS A 1060 −0.397 20.348 −16.950 1.00 1.00 O ATOM 1349 CB LYS A 1060 −1.126 20.947 −13.863 1.00 1.00 C ATOM 1350 CG LYS A 1060 −0.898 20.840 −12.321 1.00 1.00 C ATOM 1351 CD LYS A 1060 −1.557 22.027 −11.553 1.00 1.00 C ATOM 1352 CE LYS A 1060 −1.442 21.706 −10.044 1.00 1.00 C ATOM 1353 NZ LYS A 1060 −2.141 20.465 −9.627 1.00 1.00 N ATOM 1354 HA LYS A 1060 −1.167 18.737 −14.326 1.00 1.00 H ATOM 1355 HB1 LYS A 1060 −0.616 21.829 −14.236 1.00 1.00 H ATOM 1356 HB2 LYS A 1060 −2.146 20.983 −14.077 1.00 1.00 H ATOM 1357 HG1 LYS A 1060 −1.307 19.896 −12.043 1.00 1.00 H ATOM 1358 HG2 LYS A 1060 0.200 20.828 −12.094 1.00 1.00 H ATOM 1359 HD1 LYS A 1060 −1.133 22.988 −11.845 1.00 1.00 H ATOM 1360 HD2 LYS A 1060 −2.593 22.015 −11.860 1.00 1.00 H ATOM 1361 HE1 LYS A 1060 −1.827 22.565 −9.461 1.00 1.00 H ATOM 1362 HE2 LYS A 1060 −0.362 21.578 −9.737 1.00 1.00 H ATOM 1363 HZ1 LYS A 1060 −3.201 20.439 −9.913 1.00 1.00 H ATOM 1364 HZ2 LYS A 1060 −1.727 19.517 −10.033 1.00 1.00 H ATOM 1365 HZ3 LYS A 1060 −2.045 20.337 −8.558 1.00 1.00 H ATOM 1366 HN LYS A 1060 1.338 20.411 −14.681 1.00 1.00 H ATOM 1367 N PHE A 1061 −2.443 19.579 −16.367 1.00 1.00 N ATOM 1368 CA PHE A 1061 −3.006 19.744 −17.671 1.00 1.00 C ATOM 1369 C PHE A 1061 −4.526 19.639 −17.532 1.00 1.00 C ATOM 1370 O PHE A 1061 −5.023 18.972 −16.635 1.00 1.00 O ATOM 1371 CB PHE A 1061 −2.537 18.663 −18.668 1.00 1.00 C ATOM 1372 CG PHE A 1061 −3.201 18.897 −20.024 1.00 1.00 C ATOM 1373 CD1 PHE A 1061 −4.235 18.094 −20.548 1.00 1.00 C ATOM 1374 CD2 PHE A 1061 −2.699 19.923 −20.879 1.00 1.00 C ATOM 1375 CE1 PHE A 1061 −4.803 18.328 −21.816 1.00 1.00 C ATOM 1376 CE2 PHE A 1061 −3.329 20.172 −22.124 1.00 1.00 C ATOM 1377 CZ PHE A 1061 −4.398 19.402 −22.593 1.00 1.00 C ATOM 1378 HA PHE A 1061 −2.705 20.716 −18.149 1.00 1.00 H ATOM 1379 HB1 PHE A 1061 −1.450 18.746 −18.725 1.00 1.00 H ATOM 1380 HB2 PHE A 1061 −2.862 17.631 −18.258 1.00 1.00 H ATOM 1381 HD2 PHE A 1061 −1.871 20.513 −20.596 1.00 1.00 H ATOM 1382 HE2 PHE A 1061 −2.987 21.030 −22.782 1.00 1.00 H ATOM 1383 HZ PHE A 1061 −4.890 19.642 −23.520 1.00 1.00 H ATOM 1384 HE1 PHE A 1061 −5.537 17.628 −22.184 1.00 1.00 H ATOM 1385 HD1 PHE A 1061 −4.632 17.304 −19.909 1.00 1.00 H ATOM 1386 HN PHE A 1061 −3.049 19.272 −15.627 1.00 1.00 H ATOM 1387 N ALA A 1062 −5.376 20.284 −18.349 1.00 1.00 N ATOM 1388 CA ALA A 1062 −6.871 20.160 −18.256 1.00 1.00 C ATOM 1389 C ALA A 1062 −7.497 18.904 −18.742 1.00 1.00 C ATOM 1390 O ALA A 1062 −7.107 18.453 −19.815 1.00 1.00 O ATOM 1391 CB ALA A 1062 −7.550 21.504 −18.742 1.00 1.00 C ATOM 1392 HA ALA A 1062 −7.044 20.137 −17.179 1.00 1.00 H ATOM 1393 HB1 ALA A 1062 −8.643 21.417 −18.713 1.00 1.00 H ATOM 1394 HB2 ALA A 1062 −7.194 22.384 −18.132 1.00 1.00 H ATOM 1395 HB3 ALA A 1062 −7.335 21.666 −19.792 1.00 1.00 H ATOM 1396 HN ALA A 1062 −4.973 20.784 −19.105 1.00 1.00 H ATOM 1397 N VAL A 1063 −8.508 18.281 −18.001 1.00 1.00 N ATOM 1398 CA VAL A 1063 −9.127 16.996 −18.375 1.00 1.00 C ATOM 1399 C VAL A 1063 −10.646 17.053 −18.223 1.00 1.00 C ATOM 1400 O VAL A 1063 −11.223 16.324 −17.448 1.00 1.00 O ATOM 1401 CB VAL A 1063 −8.458 15.798 −17.605 1.00 1.00 C ATOM 1402 CG1 VAL A 1063 −8.673 14.424 −18.315 1.00 1.00 C ATOM 1403 CG2 VAL A 1063 −6.924 15.981 −17.482 1.00 1.00 C ATOM 1404 HA VAL A 1063 −8.935 16.772 −19.411 1.00 1.00 H ATOM 1405 HB VAL A 1063 −8.824 15.769 −16.567 1.00 1.00 H ATOM 1406 HG11 VAL A 1063 −8.184 14.491 −19.271 1.00 1.00 H ATOM 1407 HG12 VAL A 1063 −8.254 13.558 −17.758 1.00 1.00 H ATOM 1408 HG13 VAL A 1063 −9.734 14.273 −18.452 1.00 1.00 H ATOM 1409 HG21 VAL A 1063 −6.694 16.708 −16.721 1.00 1.00 H ATOM 1410 HG22 VAL A 1063 −6.380 15.014 −17.263 1.00 1.00 H ATOM 1411 HG23 VAL A 1063 −6.495 16.276 −18.419 1.00 1.00 H ATOM 1412 HN VAL A 1063 −8.862 18.752 −17.242 1.00 1.00 H ATOM 1413 N PRO A 1064 −11.422 17.810 −19.050 1.00 1.00 N ATOM 1414 CA PRO A 1064 −12.896 17.729 −19.072 1.00 1.00 C ATOM 1415 C PRO A 1064 −13.379 16.327 −19.270 1.00 1.00 C ATOM 1416 O PRO A 1064 −14.451 16.018 −18.805 1.00 1.00 O ATOM 1417 CB PRO A 1064 −13.215 18.655 −20.320 1.00 1.00 C ATOM 1418 CG PRO A 1064 −12.035 19.651 −20.380 1.00 1.00 C ATOM 1419 CD PRO A 1064 −10.832 18.727 −20.001 1.00 1.00 C ATOM 1420 HA PRO A 1064 −13.353 18.213 −18.137 1.00 1.00 H ATOM 1421 HD2 PRO A 1064 −10.376 18.193 −20.883 1.00 1.00 H ATOM 1422 HD1 PRO A 1064 −10.059 19.413 −19.567 1.00 1.00 H ATOM 1423 HG2 PRO A 1064 −11.862 20.242 −21.329 1.00 1.00 H ATOM 1424 HG1 PRO A 1064 −12.194 20.321 −19.520 1.00 1.00 H ATOM 1425 HB1 PRO A 1064 −13.191 18.082 −21.270 1.00 1.00 H ATOM 1426 HB2 PRO A 1064 −14.212 19.142 −20.220 1.00 1.00 H ATOM 1427 N ASN A 1065 −12.568 15.451 −19.888 1.00 1.00 N ATOM 1428 CA ASN A 1065 −12.982 14.084 −20.047 1.00 1.00 C ATOM 1429 C ASN A 1065 −13.510 13.475 −18.724 1.00 1.00 C ATOM 1430 O ASN A 1065 −14.505 12.758 −18.779 1.00 1.00 O ATOM 1431 CB ASN A 1065 −11.938 13.171 −20.681 1.00 1.00 C ATOM 1432 CG ASN A 1065 −12.414 11.736 −20.606 1.00 1.00 C ATOM 1433 OD1 ASN A 1065 −13.417 11.462 −21.244 1.00 1.00 O ATOM 1434 ND2 ASN A 1065 −11.740 10.868 −19.838 1.00 1.00 N ATOM 1435 HA ASN A 1065 −13.846 14.065 −20.750 1.00 1.00 H ATOM 1436 HB1 ASN A 1065 −11.873 13.466 −21.790 1.00 1.00 H ATOM 1437 HB2 ASN A 1065 −10.984 13.289 −20.213 1.00 1.00 H ATOM 1438 HD22 ASN A 1065 −11.938 9.867 −19.863 1.00 1.00 H ATOM 1439 HD21 ASN A 1065 −10.931 11.116 −19.276 1.00 1.00 H ATOM 1440 HN ASN A 1065 −11.682 15.752 −20.268 1.00 1.00 H ATOM 1441 N LEU A 1066 −12.865 13.747 −17.595 1.00 1.00 N ATOM 1442 CA LEU A 1066 −13.406 13.181 −16.401 1.00 1.00 C ATOM 1443 C LEU A 1066 −14.839 13.581 −16.191 1.00 1.00 C ATOM 1444 O LEU A 1066 −15.673 12.707 −16.066 1.00 1.00 O ATOM 1445 CB LEU A 1066 −12.637 13.545 −15.112 1.00 1.00 C ATOM 1446 CG LEU A 1066 −11.130 13.449 −15.083 1.00 1.00 C ATOM 1447 CD1 LEU A 1066 −10.571 13.752 −13.678 1.00 1.00 C ATOM 1448 CD2 LEU A 1066 −10.473 12.150 −15.604 1.00 1.00 C ATOM 1449 HA LEU A 1066 −13.235 12.093 −16.596 1.00 1.00 H ATOM 1450 HB1 LEU A 1066 −12.862 14.580 −14.804 1.00 1.00 H ATOM 1451 HB2 LEU A 1066 −13.011 12.894 −14.286 1.00 1.00 H ATOM 1452 HG LEU A 1066 −10.739 14.317 −15.655 1.00 1.00 H ATOM 1453 HD21 LEU A 1066 −10.727 11.316 −14.940 1.00 1.00 H ATOM 1454 HD22 LEU A 1066 −10.799 11.894 −16.596 1.00 1.00 H ATOM 1455 HD23 LEU A 1066 −9.364 12.291 −15.642 1.00 1.00 H ATOM 1456 HD11 LEU A 1066 −9.526 13.536 −13.570 1.00 1.00 H ATOM 1457 HD12 LEU A 1066 −10.796 14.780 −13.332 1.00 1.00 H ATOM 1458 HD13 LEU A 1066 −11.014 13.114 −12.952 1.00 1.00 H ATOM 1459 HN LEU A 1066 −12.041 14.308 −17.614 1.00 1.00 H ATOM 1460 N GLN A 1067 −15.150 14.911 −16.256 1.00 1.00 N ATOM 1461 CA GLN A 1067 −16.538 15.356 −16.167 1.00 1.00 C ATOM 1462 C GLN A 1067 −17.365 14.534 −17.142 1.00 1.00 C ATOM 1463 O GLN A 1067 −18.418 14.037 −16.810 1.00 1.00 O ATOM 1464 CB GLN A 1067 −16.703 16.830 −16.495 1.00 1.00 C ATOM 1465 CG GLN A 1067 −18.066 17.498 −16.197 1.00 1.00 C ATOM 1466 CD GLN A 1067 −18.107 18.949 −16.604 1.00 1.00 C ATOM 1467 OE1 GLN A 1067 −18.791 19.271 −17.575 1.00 1.00 O ATOM 1468 NE2 GLN A 1067 −17.347 19.886 −16.047 1.00 1.00 N ATOM 1469 HA GLN A 1067 −16.907 15.133 −15.198 1.00 1.00 H ATOM 1470 HB1 GLN A 1067 −16.002 17.396 −15.924 1.00 1.00 H ATOM 1471 HB2 GLN A 1067 −16.447 17.028 −17.540 1.00 1.00 H ATOM 1472 HG1 GLN A 1067 −18.915 16.973 −16.654 1.00 1.00 H ATOM 1473 HG2 GLN A 1067 −18.202 17.434 −15.107 1.00 1.00 H ATOM 1474 HE22 GLN A 1067 −17.377 20.838 −16.366 1.00 1.00 H ATOM 1475 HE21 GLN A 1067 −16.813 19.704 −15.203 1.00 1.00 H ATOM 1476 HN GLN A 1067 −14.432 15.621 −16.385 1.00 1.00 H ATOM 1477 N SER A 1068 −16.889 14.337 −18.407 1.00 1.00 N ATOM 1478 CA SER A 1068 −17.773 13.622 −19.384 1.00 1.00 C ATOM 1479 C SER A 1068 −18.008 12.165 −19.084 1.00 1.00 C ATOM 1480 O SER A 1068 −19.095 11.592 −19.226 1.00 1.00 O ATOM 1481 CB SER A 1068 −17.309 13.909 −20.799 1.00 1.00 C ATOM 1482 OG SER A 1068 −18.173 13.426 −21.871 1.00 1.00 O ATOM 1483 HA SER A 1068 −18.808 14.094 −19.266 1.00 1.00 H ATOM 1484 HB1 SER A 1068 −17.311 14.988 −20.829 1.00 1.00 H ATOM 1485 HB2 SER A 1068 −16.295 13.469 −20.861 1.00 1.00 H ATOM 1486 HG SER A 1068 −19.085 13.706 −21.793 1.00 1.00 H ATOM 1487 HN SER A 1068 −15.985 14.647 −18.638 1.00 1.00 H ATOM 1488 N LEU A 1069 −16.982 11.406 −18.611 1.00 1.00 N ATOM 1489 CA LEU A 1069 −17.213 10.002 −18.299 1.00 1.00 C ATOM 1490 C LEU A 1069 −18.036 9.969 −17.037 1.00 1.00 C ATOM 1491 O LEU A 1069 −18.896 9.116 −16.855 1.00 1.00 O ATOM 1492 CB LEU A 1069 −15.916 9.197 −18.064 1.00 1.00 C ATOM 1493 CG LEU A 1069 −14.996 8.946 −19.312 1.00 1.00 C ATOM 1494 CD1 LEU A 1069 −13.834 8.026 −18.890 1.00 1.00 C ATOM 1495 CD2 LEU A 1069 −15.738 8.383 −20.580 1.00 1.00 C ATOM 1496 HA LEU A 1069 −17.773 9.460 −19.077 1.00 1.00 H ATOM 1497 HB1 LEU A 1069 −15.378 9.642 −17.234 1.00 1.00 H ATOM 1498 HB2 LEU A 1069 −16.288 8.271 −17.596 1.00 1.00 H ATOM 1499 HG LEU A 1069 −14.643 9.969 −19.480 1.00 1.00 H ATOM 1500 HD21 LEU A 1069 −15.985 7.349 −20.479 1.00 1.00 H ATOM 1501 HD22 LEU A 1069 −16.611 8.972 −20.865 1.00 1.00 H ATOM 1502 HD23 LEU A 1069 −14.997 8.453 −21.386 1.00 1.00 H ATOM 1503 HD11 LEU A 1069 −13.307 8.421 −17.997 1.00 1.00 H ATOM 1504 HD12 LEU A 1069 −14.233 7.001 −18.707 1.00 1.00 H ATOM 1505 HD13 LEU A 1069 −13.094 7.905 −19.712 1.00 1.00 H ATOM 1506 HN LEU A 1069 −16.145 11.855 −18.331 1.00 1.00 H ATOM 1507 N THR A 1070 −17.788 10.870 −16.029 1.00 1.00 N ATOM 1508 CA THR A 1070 −18.693 10.799 −14.854 1.00 1.00 C ATOM 1509 C THR A 1070 −20.092 11.267 −15.233 1.00 1.00 C ATOM 1510 O THR A 1070 −21.049 10.624 −14.863 1.00 1.00 O ATOM 1511 CB THR A 1070 −18.158 11.669 −13.675 1.00 1.00 C ATOM 1512 OG1 THR A 1070 −17.813 12.974 −14.087 1.00 1.00 O ATOM 1513 CG2 THR A 1070 −16.890 10.959 −13.143 1.00 1.00 C ATOM 1514 HA THR A 1070 −18.734 9.770 −14.454 1.00 1.00 H ATOM 1515 HB THR A 1070 −18.878 11.684 −12.864 1.00 1.00 H ATOM 1516 HG1 THR A 1070 −18.524 13.554 −14.323 1.00 1.00 H ATOM 1517 HG23 THR A 1070 −17.042 9.976 −12.604 1.00 1.00 H ATOM 1518 HG21 THR A 1070 −16.118 10.871 −13.957 1.00 1.00 H ATOM 1519 HG22 THR A 1070 −16.506 11.619 −12.344 1.00 1.00 H ATOM 1520 HN THR A 1070 −17.178 11.648 −16.083 1.00 1.00 H ATOM 1521 N ASN A 1071 −20.295 12.290 −16.075 1.00 1.00 N ATOM 1522 CA ASN A 1071 −21.620 12.591 −16.515 1.00 1.00 C ATOM 1523 C ASN A 1071 −22.227 11.509 −17.359 1.00 1.00 C ATOM 1524 O ASN A 1071 −23.437 11.327 −17.333 1.00 1.00 O ATOM 1525 CB ASN A 1071 −21.598 13.845 −17.332 1.00 1.00 C ATOM 1526 CG ASN A 1071 −23.056 14.261 −17.569 1.00 1.00 C ATOM 1527 OD1 ASN A 1071 −23.600 14.063 −18.637 1.00 1.00 O ATOM 1528 ND2 ASN A 1071 −23.723 14.851 −16.551 1.00 1.00 N ATOM 1529 HA ASN A 1071 −22.238 12.759 −15.608 1.00 1.00 H ATOM 1530 HB1 ASN A 1071 −21.075 14.705 −16.910 1.00 1.00 H ATOM 1531 HB2 ASN A 1071 −21.101 13.620 −18.303 1.00 1.00 H ATOM 1532 HD22 ASN A 1071 −24.645 15.100 −16.739 1.00 1.00 H ATOM 1533 HD21 ASN A 1071 −23.358 15.069 −15.695 1.00 1.00 H ATOM 1534 HN ASN A 1071 −19.501 12.752 −16.457 1.00 1.00 H ATOM 1535 N LEU A 1072 −21.443 10.715 −18.128 1.00 1.00 N ATOM 1536 CA LEU A 1072 −22.077 9.573 −18.851 1.00 1.00 C ATOM 1537 C LEU A 1072 −22.399 8.431 −17.907 1.00 1.00 C ATOM 1538 O LEU A 1072 −23.510 7.911 −18.062 1.00 1.00 O ATOM 1539 CB LEU A 1072 −21.249 9.008 −20.007 1.00 1.00 C ATOM 1540 CG LEU A 1072 −21.003 9.901 −21.270 1.00 1.00 C ATOM 1541 CD1 LEU A 1072 −19.896 9.301 −22.229 1.00 1.00 C ATOM 1542 CD2 LEU A 1072 −22.365 10.046 −22.073 1.00 1.00 C ATOM 1543 HA LEU A 1072 −23.022 9.899 −19.273 1.00 1.00 H ATOM 1544 HB1 LEU A 1072 −20.242 8.828 −19.581 1.00 1.00 H ATOM 1545 HB2 LEU A 1072 −21.690 8.031 −20.312 1.00 1.00 H ATOM 1546 HG LEU A 1072 −20.578 10.873 −20.955 1.00 1.00 H ATOM 1547 HD21 LEU A 1072 −22.774 9.117 −22.385 1.00 1.00 H ATOM 1548 HD22 LEU A 1072 −23.130 10.617 −21.471 1.00 1.00 H ATOM 1549 HD23 LEU A 1072 −22.140 10.562 −23.023 1.00 1.00 H ATOM 1550 HD11 LEU A 1072 −20.204 8.316 −22.609 1.00 1.00 H ATOM 1551 HD12 LEU A 1072 −19.671 10.002 −23.055 1.00 1.00 H ATOM 1552 HD13 LEU A 1072 −18.981 9.241 −21.589 1.00 1.00 H ATOM 1553 HN LEU A 1072 −20.483 10.991 −18.262 1.00 1.00 H ATOM 1554 N LEU A 1073 −21.457 8.098 −17.000 1.00 1.00 N ATOM 1555 CA LEU A 1073 −21.692 6.990 −16.034 1.00 1.00 C ATOM 1556 C LEU A 1073 −22.939 7.405 −15.257 1.00 1.00 C ATOM 1557 O LEU A 1073 −23.826 6.566 −15.029 1.00 1.00 O ATOM 1558 CB LEU A 1073 −20.515 6.801 −15.044 1.00 1.00 C ATOM 1559 CG LEU A 1073 −20.793 5.854 −13.848 1.00 1.00 C ATOM 1560 CD1 LEU A 1073 −21.212 4.400 −14.230 1.00 1.00 C ATOM 1561 CD2 LEU A 1073 −19.526 5.798 −12.932 1.00 1.00 C ATOM 1562 HA LEU A 1073 −21.936 6.120 −16.628 1.00 1.00 H ATOM 1563 HB1 LEU A 1073 −19.698 6.473 −15.752 1.00 1.00 H ATOM 1564 HB2 LEU A 1073 −20.231 7.787 −14.600 1.00 1.00 H ATOM 1565 HG LEU A 1073 −21.642 6.346 −13.288 1.00 1.00 H ATOM 1566 HD21 LEU A 1073 −19.253 6.821 −12.562 1.00 1.00 H ATOM 1567 HD22 LEU A 1073 −19.741 5.071 −12.123 1.00 1.00 H ATOM 1568 HD23 LEU A 1073 −18.693 5.465 −13.507 1.00 1.00 H ATOM 1569 HD11 LEU A 1073 −21.501 3.850 −13.323 1.00 1.00 H ATOM 1570 HD12 LEU A 1073 −22.042 4.402 −14.922 1.00 1.00 H ATOM 1571 HD13 LEU A 1073 −20.367 3.859 −14.717 1.00 1.00 H ATOM 1572 HN LEU A 1073 −20.593 8.611 −16.946 1.00 1.00 H ATOM 1573 N SER A 1074 −23.105 8.663 −14.778 1.00 1.00 N ATOM 1574 CA SER A 1074 −24.270 9.037 −13.974 1.00 1.00 C ATOM 1575 C SER A 1074 −25.586 8.734 −14.640 1.00 1.00 C ATOM 1576 O SER A 1074 −26.580 8.398 −14.004 1.00 1.00 O ATOM 1577 CB SER A 1074 −24.189 10.516 −13.553 1.00 1.00 C ATOM 1578 OG SER A 1074 −24.158 11.449 −14.688 1.00 1.00 O ATOM 1579 HA SER A 1074 −24.195 8.412 −13.040 1.00 1.00 H ATOM 1580 HB1 SER A 1074 −25.012 10.675 −12.811 1.00 1.00 H ATOM 1581 HB2 SER A 1074 −23.255 10.616 −12.985 1.00 1.00 H ATOM 1582 HG SER A 1074 −24.910 11.421 −15.263 1.00 1.00 H ATOM 1583 HN SER A 1074 −22.440 9.376 −15.019 1.00 1.00 H ATOM 1584 N SER A 1075 −25.671 8.822 −16.003 1.00 1.00 N ATOM 1585 CA SER A 1075 −26.908 8.384 −16.683 1.00 1.00 C ATOM 1586 C SER A 1075 −27.038 6.932 −16.834 1.00 1.00 C ATOM 1587 O SER A 1075 −28.150 6.547 −17.078 1.00 1.00 O ATOM 1588 CB SER A 1075 −27.145 9.028 −18.092 1.00 1.00 C ATOM 1589 OG SER A 1075 −26.213 8.440 −19.054 1.00 1.00 O ATOM 1590 HA SER A 1075 −27.751 8.642 −16.058 1.00 1.00 H ATOM 1591 HB1 SER A 1075 −28.171 8.861 −18.439 1.00 1.00 H ATOM 1592 HB2 SER A 1075 −27.003 10.124 −17.930 1.00 1.00 H ATOM 1593 HG SER A 1075 −25.287 8.485 −18.823 1.00 1.00 H ATOM 1594 HN SER A 1075 −24.852 9.122 −16.485 1.00 1.00 H ATOM 1595 N ASN A 1076 −26.015 6.093 −16.720 1.00 1.00 N ATOM 1596 CA ASN A 1076 −26.212 4.668 −17.150 1.00 1.00 C ATOM 1597 C ASN A 1076 −27.100 3.942 −16.086 1.00 1.00 C ATOM 1598 O ASN A 1076 −27.814 3.057 −16.527 1.00 1.00 O ATOM 1599 CB ASN A 1076 −24.893 3.876 −17.506 1.00 1.00 C ATOM 1600 CG ASN A 1076 −24.383 4.158 −18.910 1.00 1.00 C ATOM 1601 OD1 ASN A 1076 −24.482 3.238 −19.682 1.00 1.00 O ATOM 1602 ND2 ASN A 1076 −23.746 5.344 −19.196 1.00 1.00 N ATOM 1603 HA ASN A 1076 −26.789 4.638 −18.082 1.00 1.00 H ATOM 1604 HB1 ASN A 1076 −24.145 4.157 −16.738 1.00 1.00 H ATOM 1605 HB2 ASN A 1076 −24.987 2.789 −17.418 1.00 1.00 H ATOM 1606 HD22 ASN A 1076 −23.304 5.548 −20.090 1.00 1.00 H ATOM 1607 HD21 ASN A 1076 −23.665 6.073 −18.509 1.00 1.00 H ATOM 1608 HN ASN A 1076 −25.082 6.410 −16.529 1.00 1.00 H ATOM 1609 N LEU A 1077 −26.892 4.268 −14.798 1.00 1.00 N ATOM 1610 CA LEU A 1077 −27.718 3.742 −13.686 1.00 1.00 C ATOM 1611 C LEU A 1077 −27.705 2.229 −13.514 1.00 1.00 C ATOM 1612 O LEU A 1077 −27.660 1.448 −14.460 1.00 1.00 O ATOM 1613 CB LEU A 1077 −29.119 4.307 −13.693 1.00 1.00 C ATOM 1614 CG LEU A 1077 −29.131 5.881 −13.614 1.00 1.00 C ATOM 1615 CD1 LEU A 1077 −30.570 6.428 −13.896 1.00 1.00 C ATOM 1616 CD2 LEU A 1077 −28.611 6.504 −12.313 1.00 1.00 C ATOM 1617 HA LEU A 1077 −27.185 4.095 −12.806 1.00 1.00 H ATOM 1618 HB1 LEU A 1077 −29.700 3.805 −12.898 1.00 1.00 H ATOM 1619 HB2 LEU A 1077 −29.574 4.040 −14.668 1.00 1.00 H ATOM 1620 HG LEU A 1077 −28.487 6.203 −14.444 1.00 1.00 H ATOM 1621 HD21 LEU A 1077 −29.214 6.241 −11.413 1.00 1.00 H ATOM 1622 HD22 LEU A 1077 −27.534 6.306 −12.105 1.00 1.00 H ATOM 1623 HD23 LEU A 1077 −28.764 7.603 −12.335 1.00 1.00 H ATOM 1624 HD11 LEU A 1077 −31.246 5.940 −13.192 1.00 1.00 H ATOM 1625 HD12 LEU A 1077 −30.777 6.215 −14.975 1.00 1.00 H ATOM 1626 HD13 LEU A 1077 −30.554 7.543 −13.754 1.00 1.00 H ATOM 1627 HN LEU A 1077 −26.184 4.923 −14.573 1.00 1.00 H ATOM 1628 N SER A 1078 −27.860 1.697 −12.237 1.00 1.00 N ATOM 1629 CA SER A 1078 −28.170 0.278 −12.056 1.00 1.00 C ATOM 1630 C SER A 1078 −27.111 −0.740 −12.442 1.00 1.00 C ATOM 1631 O SER A 1078 −27.277 −1.430 −13.423 1.00 1.00 O ATOM 1632 CB SER A 1078 −29.579 0.024 −12.646 1.00 1.00 C ATOM 1633 OG SER A 1078 −29.988 −1.351 −12.420 1.00 1.00 O ATOM 1634 HA SER A 1078 −28.324 0.115 −10.945 1.00 1.00 H ATOM 1635 HB1 SER A 1078 −30.237 0.799 −12.194 1.00 1.00 H ATOM 1636 HB2 SER A 1078 −29.572 0.240 −13.724 1.00 1.00 H ATOM 1637 HG SER A 1078 −30.863 −1.441 −12.775 1.00 1.00 H ATOM 1638 HN SER A 1078 −27.887 2.327 −11.431 1.00 1.00 H ATOM 1639 N TRP A 1079 −25.978 −0.964 −11.681 1.00 1.00 N ATOM 1640 CA TRP A 1079 −24.970 −1.975 −12.051 1.00 1.00 C ATOM 1641 C TRP A 1079 −23.943 −2.343 −10.975 1.00 1.00 C ATOM 1642 O TRP A 1079 −24.295 −3.091 −10.115 1.00 1.00 O ATOM 1643 CB TRP A 1079 −24.363 −1.916 −13.507 1.00 1.00 C ATOM 1644 CG TRP A 1079 −24.015 −0.585 −14.068 1.00 1.00 C ATOM 1645 CD1 TRP A 1079 −24.469 0.642 −13.698 1.00 1.00 C ATOM 1646 CD2 TRP A 1079 −23.076 −0.401 −15.236 1.00 1.00 C ATOM 1647 NE1 TRP A 1079 −23.955 1.511 −14.502 1.00 1.00 N ATOM 1648 CE2 TRP A 1079 −23.161 0.950 −15.404 1.00 1.00 C ATOM 1649 CE3 TRP A 1079 −22.270 −1.211 −16.007 1.00 1.00 C ATOM 1650 CZ2 TRP A 1079 −22.431 1.550 −16.461 1.00 1.00 C ATOM 1651 CZ3 TRP A 1079 −21.596 −0.625 −17.088 1.00 1.00 C ATOM 1652 CH2 TRP A 1079 −21.705 0.732 −17.375 1.00 1.00 C ATOM 1653 HA TRP A 1079 −25.500 −2.912 −12.104 1.00 1.00 H ATOM 1654 HB1 TRP A 1079 −23.435 −2.509 −13.504 1.00 1.00 H ATOM 1655 HB2 TRP A 1079 −24.991 −2.388 −14.328 1.00 1.00 H ATOM 1656 HE1 TRP A 1079 −24.114 2.532 −14.425 1.00 1.00 H ATOM 1657 HD1 TRP A 1079 −25.080 0.952 −12.854 1.00 1.00 H ATOM 1658 HZ2 TRP A 1079 −22.428 2.616 −16.591 1.00 1.00 H ATOM 1659 HH2 TRP A 1079 −21.252 1.117 −18.249 1.00 1.00 H ATOM 1660 HZ3 TRP A 1079 −20.920 −1.220 −17.690 1.00 1.00 H ATOM 1661 HE3 TRP A 1079 −22.054 −2.266 −15.801 1.00 1.00 H ATOM 1662 HN TRP A 1079 −25.762 −0.423 −10.837 1.00 1.00 H ATOM 1663 N LEU A 1080 −22.700 −1.792 −11.089 1.00 1.00 N ATOM 1664 CA LEU A 1080 −21.584 −2.254 −10.268 1.00 1.00 C ATOM 1665 C LEU A 1080 −20.811 −1.101 −9.688 1.00 1.00 C ATOM 1666 O LEU A 1080 −20.950 0.005 −10.133 1.00 1.00 O ATOM 1667 CB LEU A 1080 −20.441 −3.016 −11.017 1.00 1.00 C ATOM 1668 CG LEU A 1080 −20.826 −4.258 −11.883 1.00 1.00 C ATOM 1669 CD1 LEU A 1080 −19.588 −4.881 −12.618 1.00 1.00 C ATOM 1670 CD2 LEU A 1080 −21.377 −5.336 −10.920 1.00 1.00 C ATOM 1671 HA LEU A 1080 −21.889 −2.916 −9.459 1.00 1.00 H ATOM 1672 HB1 LEU A 1080 −19.960 −2.303 −11.744 1.00 1.00 H ATOM 1673 HB2 LEU A 1080 −19.667 −3.281 −10.340 1.00 1.00 H ATOM 1674 HG LEU A 1080 −21.643 −4.010 −12.587 1.00 1.00 H ATOM 1675 HD21 LEU A 1080 −22.341 −5.020 −10.582 1.00 1.00 H ATOM 1676 HD22 LEU A 1080 −20.689 −5.488 −10.085 1.00 1.00 H ATOM 1677 HD23 LEU A 1080 −21.477 −6.373 −11.317 1.00 1.00 H ATOM 1678 HD11 LEU A 1080 −18.733 −5.130 −11.971 1.00 1.00 H ATOM 1679 HD12 LEU A 1080 −19.232 −4.119 −13.335 1.00 1.00 H ATOM 1680 HD13 LEU A 1080 −19.893 −5.784 −13.153 1.00 1.00 H ATOM 1681 HN LEU A 1080 −22.490 −1.072 −11.757 1.00 1.00 H ATOM 1682 N SER A 1081 −19.941 −1.344 −8.681 1.00 1.00 N ATOM 1683 CA SER A 1081 −18.991 −0.360 −8.239 1.00 1.00 C ATOM 1684 C SER A 1081 −17.758 −1.005 −7.602 1.00 1.00 C ATOM 1685 O SER A 1081 −17.930 −1.894 −6.811 1.00 1.00 O ATOM 1686 CB SER A 1081 −19.537 0.505 −7.057 1.00 1.00 C ATOM 1687 OG SER A 1081 −20.625 1.320 −7.482 1.00 1.00 O ATOM 1688 HA SER A 1081 −18.636 0.244 −9.061 1.00 1.00 H ATOM 1689 HB1 SER A 1081 −18.758 1.185 −6.666 1.00 1.00 H ATOM 1690 HB2 SER A 1081 −19.856 −0.125 −6.196 1.00 1.00 H ATOM 1691 HG SER A 1081 −21.039 1.885 −6.839 1.00 1.00 H ATOM 1692 HN SER A 1081 −20.022 −2.240 −8.215 1.00 1.00 H ATOM 1693 N LEU A 1082 −16.475 −0.608 −7.969 1.00 1.00 N ATOM 1694 CA LEU A 1082 −15.313 −1.365 −7.516 1.00 1.00 C ATOM 1695 C LEU A 1082 −14.034 −0.533 −7.285 1.00 1.00 C ATOM 1696 O LEU A 1082 −13.521 −0.053 −8.242 1.00 1.00 O ATOM 1697 CB LEU A 1082 −15.143 −2.463 −8.695 1.00 1.00 C ATOM 1698 CG LEU A 1082 −13.786 −3.220 −8.647 1.00 1.00 C ATOM 1699 CD1 LEU A 1082 −13.527 −3.801 −7.229 1.00 1.00 C ATOM 1700 CD2 LEU A 1082 −13.707 −4.324 −9.760 1.00 1.00 C ATOM 1701 HA LEU A 1082 −15.479 −1.967 −6.595 1.00 1.00 H ATOM 1702 HB1 LEU A 1082 −15.184 −1.967 −9.666 1.00 1.00 H ATOM 1703 HB2 LEU A 1082 −15.980 −3.250 −8.697 1.00 1.00 H ATOM 1704 HG LEU A 1082 −13.011 −2.502 −8.889 1.00 1.00 H ATOM 1705 HD21 LEU A 1082 −14.460 −5.095 −9.520 1.00 1.00 H ATOM 1706 HD22 LEU A 1082 −13.856 −3.903 −10.740 1.00 1.00 H ATOM 1707 HD23 LEU A 1082 −12.681 −4.749 −9.767 1.00 1.00 H ATOM 1708 HD11 LEU A 1082 −12.549 −4.266 −7.278 1.00 1.00 H ATOM 1709 HD12 LEU A 1082 −13.499 −3.068 −6.477 1.00 1.00 H ATOM 1710 HD13 LEU A 1082 −14.277 −4.586 −6.926 1.00 1.00 H ATOM 1711 HN LEU A 1082 −16.332 0.056 −8.714 1.00 1.00 H ATOM 1712 N ASP A 1083 −13.593 −0.411 −5.990 1.00 1.00 N ATOM 1713 CA ASP A 1083 −12.300 0.283 −5.667 1.00 1.00 C ATOM 1714 C ASP A 1083 −11.242 −0.765 −5.825 1.00 1.00 C ATOM 1715 O ASP A 1083 −11.321 −1.749 −5.077 1.00 1.00 O ATOM 1716 CB ASP A 1083 −12.082 0.955 −4.254 1.00 1.00 C ATOM 1717 CG ASP A 1083 −10.967 2.021 −3.992 1.00 1.00 C ATOM 1718 OD1 ASP A 1083 −11.119 3.207 −4.265 1.00 1.00 O ATOM 1719 OD2 ASP A 1083 −9.895 1.695 −3.449 1.00 1.00 O ATOM 1720 HA ASP A 1083 −12.198 1.111 −6.349 1.00 1.00 H ATOM 1721 HB1 ASP A 1083 −11.824 0.173 −3.539 1.00 1.00 H ATOM 1722 HB2 ASP A 1083 −13.092 1.419 −3.958 1.00 1.00 H ATOM 1723 HN ASP A 1083 −14.107 −0.766 −5.247 1.00 1.00 H ATOM 1724 N VAL A 1084 −10.275 −0.590 −6.737 1.00 1.00 N ATOM 1725 CA VAL A 1084 −9.274 −1.609 −7.015 1.00 1.00 C ATOM 1726 C VAL A 1084 −8.045 −1.410 −6.141 1.00 1.00 C ATOM 1727 O VAL A 1084 −7.072 −0.882 −6.608 1.00 1.00 O ATOM 1728 CB VAL A 1084 −8.936 −1.573 −8.549 1.00 1.00 C ATOM 1729 CG1 VAL A 1084 −7.887 −2.600 −8.987 1.00 1.00 C ATOM 1730 CG2 VAL A 1084 −10.222 −1.659 −9.421 1.00 1.00 C ATOM 1731 HA VAL A 1084 −9.709 −2.579 −6.791 1.00 1.00 H ATOM 1732 HB VAL A 1084 −8.517 −0.538 −8.771 1.00 1.00 H ATOM 1733 HG11 VAL A 1084 −8.249 −3.635 −8.833 1.00 1.00 H ATOM 1734 HG12 VAL A 1084 −7.696 −2.555 −10.060 1.00 1.00 H ATOM 1735 HG13 VAL A 1084 −6.944 −2.430 −8.436 1.00 1.00 H ATOM 1736 HG21 VAL A 1084 −10.992 −0.922 −9.120 1.00 1.00 H ATOM 1737 HG22 VAL A 1084 −9.953 −1.491 −10.505 1.00 1.00 H ATOM 1738 HG23 VAL A 1084 −10.637 −2.705 −9.367 1.00 1.00 H ATOM 1739 HN VAL A 1084 −10.181 0.333 −7.157 1.00 1.00 H ATOM 1740 N SER A 1085 −8.056 −1.897 −4.895 1.00 1.00 N ATOM 1741 CA SER A 1085 −6.850 −1.786 −4.026 1.00 1.00 C ATOM 1742 C SER A 1085 −5.691 −2.619 −4.539 1.00 1.00 C ATOM 1743 O SER A 1085 −5.266 −3.599 −3.941 1.00 1.00 O ATOM 1744 CB SER A 1085 −7.185 −2.342 −2.622 1.00 1.00 C ATOM 1745 OG SER A 1085 −6.127 −2.078 −1.636 1.00 1.00 O ATOM 1746 HA SER A 1085 −6.564 −0.698 −3.922 1.00 1.00 H ATOM 1747 HB1 SER A 1085 −7.410 −3.430 −2.696 1.00 1.00 H ATOM 1748 HB2 SER A 1085 −8.062 −1.796 −2.228 1.00 1.00 H ATOM 1749 HG SER A 1085 −5.933 −1.130 −1.502 1.00 1.00 H ATOM 1750 HN SER A 1085 −8.863 −2.359 −4.524 1.00 1.00 H ATOM 1751 N ALA A 1086 −5.034 −2.201 −5.641 1.00 1.00 N ATOM 1752 CA ALA A 1086 −3.970 −2.958 −6.273 1.00 1.00 C ATOM 1753 C ALA A 1086 −2.993 −2.122 −7.107 1.00 1.00 C ATOM 1754 O ALA A 1086 −1.818 −2.246 −6.825 1.00 1.00 O ATOM 1755 CB ALA A 1086 −4.431 −4.135 −7.198 1.00 1.00 C ATOM 1756 HA ALA A 1086 −3.401 −3.374 −5.427 1.00 1.00 H ATOM 1757 HB1 ALA A 1086 −3.508 −4.728 −7.471 1.00 1.00 H ATOM 1758 HB2 ALA A 1086 −5.062 −4.795 −6.561 1.00 1.00 H ATOM 1759 HB3 ALA A 1086 −4.971 −3.675 −8.059 1.00 1.00 H ATOM 1760 HN ALA A 1086 −5.434 −1.396 −6.140 1.00 1.00 H ATOM 1761 N ALA A 1087 −3.450 −1.371 −8.166 1.00 1.00 N ATOM 1762 CA ALA A 1087 −2.500 −0.721 −9.069 1.00 1.00 C ATOM 1763 C ALA A 1087 −1.439 0.009 −8.310 1.00 1.00 C ATOM 1764 O ALA A 1087 −0.266 −0.278 −8.550 1.00 1.00 O ATOM 1765 CB ALA A 1087 −3.196 0.299 −10.022 1.00 1.00 C ATOM 1766 HA ALA A 1087 −2.012 −1.539 −9.583 1.00 1.00 H ATOM 1767 HB1 ALA A 1087 −2.471 0.819 −10.662 1.00 1.00 H ATOM 1768 HB2 ALA A 1087 −3.858 −0.269 −10.686 1.00 1.00 H ATOM 1769 HB3 ALA A 1087 −3.736 1.076 −9.495 1.00 1.00 H ATOM 1770 HN ALA A 1087 −4.400 −1.282 −8.371 1.00 1.00 H ATOM 1771 N PHE A 1088 −1.822 0.946 −7.423 1.00 1.00 N ATOM 1772 CA PHE A 1088 −0.794 1.712 −6.728 1.00 1.00 C ATOM 1773 C PHE A 1088 −0.577 1.067 −5.338 1.00 1.00 C ATOM 1774 O PHE A 1088 −0.572 1.771 −4.350 1.00 1.00 O ATOM 1775 CB PHE A 1088 −1.168 3.159 −6.721 1.00 1.00 C ATOM 1776 CG PHE A 1088 −0.908 3.894 −8.028 1.00 1.00 C ATOM 1777 CD1 PHE A 1088 −0.468 3.296 −9.228 1.00 1.00 C ATOM 1778 CD2 PHE A 1088 −1.155 5.285 −8.039 1.00 1.00 C ATOM 1779 CE1 PHE A 1088 −0.344 4.098 −10.350 1.00 1.00 C ATOM 1780 CE2 PHE A 1088 −1.127 6.038 −9.197 1.00 1.00 C ATOM 1781 CZ PHE A 1088 −0.692 5.424 −10.383 1.00 1.00 C ATOM 1782 HA PHE A 1088 0.211 1.562 −7.138 1.00 1.00 H ATOM 1783 HB1 PHE A 1088 −0.694 3.803 −5.977 1.00 1.00 H ATOM 1784 HB2 PHE A 1088 −2.279 3.262 −6.624 1.00 1.00 H ATOM 1785 HD2 PHE A 1088 −1.361 5.772 −7.131 1.00 1.00 H ATOM 1786 HE2 PHE A 1088 −1.383 7.100 −9.235 1.00 1.00 H ATOM 1787 HZ PHE A 1088 −0.559 6.029 −11.282 1.00 1.00 H ATOM 1788 HE1 PHE A 1088 0.127 3.540 −11.213 1.00 1.00 H ATOM 1789 HD1 PHE A 1088 −0.255 2.216 −9.266 1.00 1.00 H ATOM 1790 HN PHE A 1088 −2.755 1.120 −7.230 1.00 1.00 H ATOM 1791 N TYR A 1089 −0.392 −0.288 −5.189 1.00 1.00 N ATOM 1792 CA TYR A 1089 −0.274 −0.899 −3.881 1.00 1.00 C ATOM 1793 C TYR A 1089 0.364 −2.284 −3.802 1.00 1.00 C ATOM 1794 O TYR A 1089 1.383 −2.393 −3.174 1.00 1.00 O ATOM 1795 CB TYR A 1089 −1.723 −1.008 −3.286 1.00 1.00 C ATOM 1796 CG TYR A 1089 −1.868 −0.802 −1.770 1.00 1.00 C ATOM 1797 CD1 TYR A 1089 −2.927 −0.034 −1.288 1.00 1.00 C ATOM 1798 CD2 TYR A 1089 −0.955 −1.323 −0.809 1.00 1.00 C ATOM 1799 CE1 TYR A 1089 −3.138 0.223 0.076 1.00 1.00 C ATOM 1800 CE2 TYR A 1089 −1.141 −1.045 0.555 1.00 1.00 C ATOM 1801 CZ TYR A 1089 −2.223 −0.290 1.005 1.00 1.00 C ATOM 1802 OH TYR A 1089 −2.373 −0.075 2.401 1.00 1.00 O ATOM 1803 HA TYR A 1089 0.303 −0.285 −3.220 1.00 1.00 H ATOM 1804 HB2 TYR A 1089 −2.121 −2.000 −3.539 1.00 1.00 H ATOM 1805 HB1 TYR A 1089 −2.345 −0.279 −3.752 1.00 1.00 H ATOM 1806 HD2 TYR A 1089 −0.137 −1.916 −1.153 1.00 1.00 H ATOM 1807 HE2 TYR A 1089 −0.406 −1.427 1.249 1.00 1.00 H ATOM 1808 HE1 TYR A 1089 −3.987 0.775 0.407 1.00 1.00 H ATOM 1809 HD1 TYR A 1089 −3.627 0.416 −2.005 1.00 1.00 H ATOM 1810 HH TYR A 1089 −3.116 0.484 2.621 1.00 1.00 H ATOM 1811 HN TYR A 1089 −0.525 −0.866 −5.977 1.00 1.00 H ATOM 1812 N HIS A 1090 −0.245 −3.349 −4.386 1.00 1.00 N ATOM 1813 CA HIS A 1090 0.036 −4.745 −4.070 1.00 1.00 C ATOM 1814 C HIS A 1090 0.495 −5.617 −5.216 1.00 1.00 C ATOM 1815 O HIS A 1090 −0.143 −6.618 −5.506 1.00 1.00 O ATOM 1816 CB HIS A 1090 −1.261 −5.342 −3.421 1.00 1.00 C ATOM 1817 CG HIS A 1090 −1.261 −6.785 −3.060 1.00 1.00 C ATOM 1818 ND1 HIS A 1090 −0.421 −7.296 −2.197 1.00 1.00 N ATOM 1819 CD2 HIS A 1090 −2.073 −7.786 −3.493 1.00 1.00 C ATOM 1820 CE1 HIS A 1090 −0.693 −8.555 −1.987 1.00 1.00 C ATOM 1821 NE2 HIS A 1090 −1.632 −8.926 −2.733 1.00 1.00 N ATOM 1822 HA HIS A 1090 0.830 −4.840 −3.328 1.00 1.00 H ATOM 1823 HB1 HIS A 1090 −2.017 −5.260 −4.233 1.00 1.00 H ATOM 1824 HB2 HIS A 1090 −1.513 −4.675 −2.555 1.00 1.00 H ATOM 1825 HD2 HIS A 1090 −2.827 −7.607 −4.243 1.00 1.00 H ATOM 1826 HE1 HIS A 1090 −0.118 −9.168 −1.297 1.00 1.00 H ATOM 1827 HD1 HIS A 1090 0.316 −6.808 −1.678 1.00 1.00 H ATOM 1828 HN HIS A 1090 −0.962 −3.217 −5.056 1.00 1.00 H ATOM 1829 N LEU A 1091 1.650 −5.280 −5.850 1.00 1.00 N ATOM 1830 CA LEU A 1091 2.139 −6.088 −6.984 1.00 1.00 C ATOM 1831 C LEU A 1091 3.616 −6.430 −6.942 1.00 1.00 C ATOM 1832 O LEU A 1091 4.344 −5.673 −6.286 1.00 1.00 O ATOM 1833 CB LEU A 1091 1.830 −5.255 −8.251 1.00 1.00 C ATOM 1834 CG LEU A 1091 0.299 −5.235 −8.560 1.00 1.00 C ATOM 1835 CD1 LEU A 1091 −0.079 −4.065 −9.559 1.00 1.00 C ATOM 1836 CD2 LEU A 1091 −0.133 −6.621 −9.117 1.00 1.00 C ATOM 1837 HA LEU A 1091 1.687 −7.083 −6.966 1.00 1.00 H ATOM 1838 HB1 LEU A 1091 2.348 −5.650 −9.171 1.00 1.00 H ATOM 1839 HB2 LEU A 1091 2.217 −4.217 −8.066 1.00 1.00 H ATOM 1840 HG LEU A 1091 −0.322 −5.071 −7.639 1.00 1.00 H ATOM 1841 HD21 LEU A 1091 −0.073 −7.480 −8.458 1.00 1.00 H ATOM 1842 HD22 LEU A 1091 −1.154 −6.399 −9.445 1.00 1.00 H ATOM 1843 HD23 LEU A 1091 0.457 −6.827 −10.034 1.00 1.00 H ATOM 1844 HD11 LEU A 1091 0.496 −4.148 −10.520 1.00 1.00 H ATOM 1845 HD12 LEU A 1091 −1.144 −4.138 −9.783 1.00 1.00 H ATOM 1846 HD13 LEU A 1091 0.089 −3.060 −9.098 1.00 1.00 H ATOM 1847 HN LEU A 1091 2.232 −4.502 −5.500 1.00 1.00 H ATOM 1848 N PRO A 1092 4.163 −7.526 −7.537 1.00 1.00 N ATOM 1849 CA PRO A 1092 3.354 −8.517 −8.207 1.00 1.00 C ATOM 1850 C PRO A 1092 2.776 −9.467 −7.154 1.00 1.00 C ATOM 1851 O PRO A 1092 3.219 −9.371 −6.028 1.00 1.00 O ATOM 1852 CB PRO A 1092 4.460 −9.267 −8.973 1.00 1.00 C ATOM 1853 CG PRO A 1092 5.647 −9.210 −7.963 1.00 1.00 C ATOM 1854 CD PRO A 1092 5.580 −7.789 −7.427 1.00 1.00 C ATOM 1855 HA PRO A 1092 2.528 −8.128 −8.857 1.00 1.00 H ATOM 1856 HD2 PRO A 1092 5.832 −7.757 −6.342 1.00 1.00 H ATOM 1857 HD1 PRO A 1092 6.178 −7.180 −8.092 1.00 1.00 H ATOM 1858 HG2 PRO A 1092 6.599 −9.413 −8.457 1.00 1.00 H ATOM 1859 HG1 PRO A 1092 5.491 −10.031 −7.206 1.00 1.00 H ATOM 1860 HB1 PRO A 1092 4.725 −8.743 −9.905 1.00 1.00 H ATOM 1861 HB2 PRO A 1092 4.199 −10.301 −9.271 1.00 1.00 H ATOM 1862 N LEU A 1093 1.854 −10.428 −7.421 1.00 1.00 N ATOM 1863 CA LEU A 1093 1.576 −11.535 −6.460 1.00 1.00 C ATOM 1864 C LEU A 1093 2.711 −12.545 −6.391 1.00 1.00 C ATOM 1865 O LEU A 1093 2.555 −13.721 −6.661 1.00 1.00 O ATOM 1866 CB LEU A 1093 1.015 −11.068 −5.067 1.00 1.00 C ATOM 1867 CG LEU A 1093 0.654 −12.292 −4.168 1.00 1.00 C ATOM 1868 CD1 LEU A 1093 0.544 −11.938 −2.648 1.00 1.00 C ATOM 1869 CD2 LEU A 1093 −0.666 −12.993 −4.524 1.00 1.00 C ATOM 1870 HA LEU A 1093 0.691 −12.037 −6.939 1.00 1.00 H ATOM 1871 HB1 LEU A 1093 0.122 −10.396 −5.129 1.00 1.00 H ATOM 1872 HB2 LEU A 1093 1.855 −10.516 −4.546 1.00 1.00 H ATOM 1873 HG LEU A 1093 1.492 −13.012 −4.182 1.00 1.00 H ATOM 1874 HD21 LEU A 1093 −1.561 −12.336 −4.542 1.00 1.00 H ATOM 1875 HD22 LEU A 1093 −0.580 −13.503 −5.539 1.00 1.00 H ATOM 1876 HD23 LEU A 1093 −0.845 −13.812 −3.857 1.00 1.00 H ATOM 1877 HD11 LEU A 1093 1.501 −11.650 −2.236 1.00 1.00 H ATOM 1878 HD12 LEU A 1093 −0.173 −11.132 −2.450 1.00 1.00 H ATOM 1879 HD13 LEU A 1093 0.286 −12.792 −2.071 1.00 1.00 H ATOM 1880 HN LEU A 1093 1.401 −10.426 −8.266 1.00 1.00 H ATOM 1881 N HIS A 1094 3.958 −12.140 −5.941 1.00 1.00 N ATOM 1882 CA HIS A 1094 5.150 −13.032 −5.808 1.00 1.00 C ATOM 1883 C HIS A 1094 6.114 −12.377 −4.787 1.00 1.00 C ATOM 1884 O HIS A 1094 5.943 −11.231 −4.382 1.00 1.00 O ATOM 1885 CB HIS A 1094 5.843 −13.047 −7.215 1.00 1.00 C ATOM 1886 CG HIS A 1094 5.770 −14.403 −7.842 1.00 1.00 C ATOM 1887 ND1 HIS A 1094 4.678 −15.116 −7.931 1.00 1.00 N ATOM 1888 CD2 HIS A 1094 6.798 −15.099 −8.386 1.00 1.00 C ATOM 1889 CE1 HIS A 1094 4.914 −16.253 −8.498 1.00 1.00 C ATOM 1890 NE2 HIS A 1094 6.127 −16.315 −8.758 1.00 1.00 N ATOM 1891 HA HIS A 1094 4.865 −14.054 −5.456 1.00 1.00 H ATOM 1892 HB1 HIS A 1094 6.862 −12.641 −7.126 1.00 1.00 H ATOM 1893 HB2 HIS A 1094 5.214 −12.421 −7.947 1.00 1.00 H ATOM 1894 HD2 HIS A 1094 7.888 −14.807 −8.478 1.00 1.00 H ATOM 1895 HE1 HIS A 1094 4.208 −17.033 −8.741 1.00 1.00 H ATOM 1896 HD1 HIS A 1094 3.776 −14.717 −7.645 1.00 1.00 H ATOM 1897 HN HIS A 1094 4.036 −11.130 −5.778 1.00 1.00 H ATOM 1898 N PRO A 1095 7.166 −13.095 −4.298 1.00 1.00 N ATOM 1899 CA PRO A 1095 8.168 −12.401 −3.496 1.00 1.00 C ATOM 1900 C PRO A 1095 8.949 −11.518 −4.465 1.00 1.00 C ATOM 1901 O PRO A 1095 10.075 −11.840 −4.828 1.00 1.00 O ATOM 1902 CB PRO A 1095 9.090 −13.609 −3.025 1.00 1.00 C ATOM 1903 CG PRO A 1095 8.823 −14.749 −4.054 1.00 1.00 C ATOM 1904 CD PRO A 1095 7.402 −14.492 −4.649 1.00 1.00 C ATOM 1905 HA PRO A 1095 7.772 −11.735 −2.693 1.00 1.00 H ATOM 1906 HD2 PRO A 1095 6.755 −15.160 −4.095 1.00 1.00 H ATOM 1907 HD1 PRO A 1095 7.489 −14.813 −5.720 1.00 1.00 H ATOM 1908 HG2 PRO A 1095 9.088 −15.792 −3.769 1.00 1.00 H ATOM 1909 HG1 PRO A 1095 9.530 −14.431 −4.828 1.00 1.00 H ATOM 1910 HB1 PRO A 1095 8.715 −13.957 −2.046 1.00 1.00 H ATOM 1911 HB2 PRO A 1095 10.120 −13.316 −2.847 1.00 1.00 H ATOM 1912 N ALA A 1096 8.348 −10.386 −4.929 1.00 1.00 N ATOM 1913 CA ALA A 1096 9.193 −9.454 −5.715 1.00 1.00 C ATOM 1914 C ALA A 1096 8.524 −8.133 −5.936 1.00 1.00 C ATOM 1915 O ALA A 1096 8.643 −7.596 −7.005 1.00 1.00 O ATOM 1916 CB ALA A 1096 9.412 −10.166 −7.068 1.00 1.00 C ATOM 1917 HA ALA A 1096 10.107 −9.169 −5.198 1.00 1.00 H ATOM 1918 HB1 ALA A 1096 9.896 −9.528 −7.790 1.00 1.00 H ATOM 1919 HB2 ALA A 1096 10.054 −11.099 −7.029 1.00 1.00 H ATOM 1920 HB3 ALA A 1096 8.367 −10.398 −7.377 1.00 1.00 H ATOM 1921 HN ALA A 1096 7.416 −10.166 −4.670 1.00 1.00 H ATOM 1922 N ALA A 1097 7.941 −7.531 −4.899 1.00 1.00 N ATOM 1923 CA ALA A 1097 7.477 −6.130 −5.084 1.00 1.00 C ATOM 1924 C ALA A 1097 8.756 −5.383 −4.881 1.00 1.00 C ATOM 1925 O ALA A 1097 8.986 −4.961 −3.734 1.00 1.00 O ATOM 1926 CB ALA A 1097 6.395 −5.751 −4.057 1.00 1.00 C ATOM 1927 HA ALA A 1097 7.158 −5.902 −6.122 1.00 1.00 H ATOM 1928 HB1 ALA A 1097 6.000 −4.713 −4.125 1.00 1.00 H ATOM 1929 HB2 ALA A 1097 5.566 −6.449 −4.097 1.00 1.00 H ATOM 1930 HB3 ALA A 1097 6.761 −5.823 −2.990 1.00 1.00 H ATOM 1931 HN ALA A 1097 7.984 −7.895 −3.955 1.00 1.00 H ATOM 1932 N MET A 1098 9.590 −5.193 −5.898 1.00 1.00 N ATOM 1933 CA MET A 1098 10.943 −4.773 −5.549 1.00 1.00 C ATOM 1934 C MET A 1098 11.757 −4.353 −6.768 1.00 1.00 C ATOM 1935 O MET A 1098 12.161 −3.222 −6.640 1.00 1.00 O ATOM 1936 CB MET A 1098 11.620 −5.915 −4.732 1.00 1.00 C ATOM 1937 CG MET A 1098 13.096 −5.667 −4.462 1.00 1.00 C ATOM 1938 SD MET A 1098 14.114 −5.995 −5.888 1.00 1.00 S ATOM 1939 CE MET A 1098 15.724 −5.816 −5.040 1.00 1.00 C ATOM 1940 HA MET A 1098 10.829 −3.853 −4.943 1.00 1.00 H ATOM 1941 HB1 MET A 1098 11.496 −6.913 −5.180 1.00 1.00 H ATOM 1942 HB2 MET A 1098 11.141 −5.917 −3.750 1.00 1.00 H ATOM 1943 HG1 MET A 1098 13.220 −4.645 −4.134 1.00 1.00 H ATOM 1944 HG2 MET A 1098 13.429 −6.338 −3.646 1.00 1.00 H ATOM 1945 HE1 MET A 1098 15.839 −6.469 −4.193 1.00 1.00 H ATOM 1946 HE2 MET A 1098 16.497 −6.028 −5.750 1.00 1.00 H ATOM 1947 HE3 MET A 1098 15.787 −4.777 −4.598 1.00 1.00 H ATOM 1948 HN MET A 1098 9.324 −5.528 −6.797 1.00 1.00 H ATOM 1949 N PRO A 1099 12.078 −5.082 −7.918 1.00 1.00 N ATOM 1950 CA PRO A 1099 12.964 −4.480 −8.869 1.00 1.00 C ATOM 1951 C PRO A 1099 12.765 −3.045 −9.345 1.00 1.00 C ATOM 1952 O PRO A 1099 13.725 −2.269 −9.201 1.00 1.00 O ATOM 1953 CB PRO A 1099 12.933 −5.559 −9.984 1.00 1.00 C ATOM 1954 CG PRO A 1099 12.548 −6.909 −9.282 1.00 1.00 C ATOM 1955 CD PRO A 1099 11.563 −6.436 −8.190 1.00 1.00 C ATOM 1956 HA PRO A 1099 13.955 −4.462 −8.331 1.00 1.00 H ATOM 1957 HD2 PRO A 1099 10.569 −6.455 −8.620 1.00 1.00 H ATOM 1958 HD1 PRO A 1099 11.625 −7.213 −7.388 1.00 1.00 H ATOM 1959 HG2 PRO A 1099 13.435 −7.364 −8.825 1.00 1.00 H ATOM 1960 HG1 PRO A 1099 12.126 −7.633 −9.994 1.00 1.00 H ATOM 1961 HB1 PRO A 1099 12.188 −5.404 −10.766 1.00 1.00 H ATOM 1962 HB2 PRO A 1099 13.860 −5.613 −10.533 1.00 1.00 H ATOM 1963 N HIS A 1100 11.613 −2.563 −9.875 1.00 1.00 N ATOM 1964 CA HIS A 1100 10.370 −3.347 −10.064 1.00 1.00 C ATOM 1965 C HIS A 1100 10.313 −3.602 −11.518 1.00 1.00 C ATOM 1966 O HIS A 1100 10.715 −2.796 −12.332 1.00 1.00 O ATOM 1967 CB HIS A 1100 9.130 −2.485 −9.611 1.00 1.00 C ATOM 1968 CG HIS A 1100 7.828 −3.147 −9.907 1.00 1.00 C ATOM 1969 ND1 HIS A 1100 7.276 −4.121 −9.235 1.00 1.00 N ATOM 1970 CD2 HIS A 1100 6.995 −2.806 −10.896 1.00 1.00 C ATOM 1971 CE1 HIS A 1100 6.115 −4.425 −9.738 1.00 1.00 C ATOM 1972 NE2 HIS A 1100 5.876 −3.721 −10.753 1.00 1.00 N ATOM 1973 HA HIS A 1100 10.301 −4.270 −9.498 1.00 1.00 H ATOM 1974 HB1 HIS A 1100 9.022 −1.488 −10.110 1.00 1.00 H ATOM 1975 HB2 HIS A 1100 9.274 −2.271 −8.529 1.00 1.00 H ATOM 1976 HD2 HIS A 1100 7.198 −2.024 −11.608 1.00 1.00 H ATOM 1977 HE1 HIS A 1100 5.403 −5.126 −9.381 1.00 1.00 H ATOM 1978 HD1 HIS A 1100 7.646 −4.498 −8.335 1.00 1.00 H ATOM 1979 HN HIS A 1100 11.669 −1.604 −10.247 1.00 1.00 H ATOM 1980 N LEU A 1101 9.803 −4.799 −11.966 1.00 1.00 N ATOM 1981 CA LEU A 1101 9.774 −5.140 −13.423 1.00 1.00 C ATOM 1982 C LEU A 1101 8.608 −6.009 −13.780 1.00 1.00 C ATOM 1983 O LEU A 1101 8.877 −7.053 −14.342 1.00 1.00 O ATOM 1984 CB LEU A 1101 11.194 −5.679 −13.669 1.00 1.00 C ATOM 1985 CG LEU A 1101 11.562 −6.050 −15.134 1.00 1.00 C ATOM 1986 CD1 LEU A 1101 11.631 −4.733 −15.996 1.00 1.00 C ATOM 1987 CD2 LEU A 1101 12.999 −6.668 −15.146 1.00 1.00 C ATOM 1988 HA LEU A 1101 9.683 −4.231 −14.079 1.00 1.00 H ATOM 1989 HB1 LEU A 1101 11.381 −6.545 −12.971 1.00 1.00 H ATOM 1990 HB2 LEU A 1101 11.926 −4.942 −13.286 1.00 1.00 H ATOM 1991 HG LEU A 1101 10.849 −6.784 −15.543 1.00 1.00 H ATOM 1992 HD21 LEU A 1101 13.729 −6.052 −14.526 1.00 1.00 H ATOM 1993 HD22 LEU A 1101 12.896 −7.666 −14.661 1.00 1.00 H ATOM 1994 HD23 LEU A 1101 13.429 −6.768 −16.191 1.00 1.00 H ATOM 1995 HD11 LEU A 1101 10.673 −4.215 −16.025 1.00 1.00 H ATOM 1996 HD12 LEU A 1101 12.368 −4.046 −15.550 1.00 1.00 H ATOM 1997 HD13 LEU A 1101 11.848 −4.956 −17.020 1.00 1.00 H ATOM 1998 HN LEU A 1101 9.601 −5.577 −11.415 1.00 1.00 H ATOM 1999 N LEU A 1102 7.373 −5.552 −13.390 1.00 1.00 N ATOM 2000 CA LEU A 1102 6.202 −6.364 −13.741 1.00 1.00 C ATOM 2001 C LEU A 1102 5.805 −6.124 −15.209 1.00 1.00 C ATOM 2002 O LEU A 1102 5.408 −4.991 −15.419 1.00 1.00 O ATOM 2003 CB LEU A 1102 4.997 −5.992 −12.804 1.00 1.00 C ATOM 2004 CG LEU A 1102 3.655 −6.723 −13.169 1.00 1.00 C ATOM 2005 CD1 LEU A 1102 3.715 −8.290 −13.243 1.00 1.00 C ATOM 2006 CD2 LEU A 1102 2.570 −6.309 −12.150 1.00 1.00 C ATOM 2007 HA LEU A 1102 6.469 −7.426 −13.627 1.00 1.00 H ATOM 2008 HB1 LEU A 1102 4.865 −4.886 −12.897 1.00 1.00 H ATOM 2009 HB2 LEU A 1102 5.326 −6.317 −11.819 1.00 1.00 H ATOM 2010 HG LEU A 1102 3.306 −6.365 −14.186 1.00 1.00 H ATOM 2011 HD21 LEU A 1102 2.846 −6.751 −11.166 1.00 1.00 H ATOM 2012 HD22 LEU A 1102 2.527 −5.210 −12.093 1.00 1.00 H ATOM 2013 HD23 LEU A 1102 1.599 −6.753 −12.410 1.00 1.00 H ATOM 2014 HD11 LEU A 1102 2.830 −8.690 −13.775 1.00 1.00 H ATOM 2015 HD12 LEU A 1102 4.592 −8.547 −13.880 1.00 1.00 H ATOM 2016 HD13 LEU A 1102 3.878 −8.818 −12.305 1.00 1.00 H ATOM 2017 HN LEU A 1102 7.327 −4.708 −12.845 1.00 1.00 H ATOM 2018 N VAL A 1103 5.893 −7.139 −16.130 1.00 1.00 N ATOM 2019 CA VAL A 1103 5.352 −6.960 −17.468 1.00 1.00 C ATOM 2020 C VAL A 1103 4.650 −8.238 −17.904 1.00 1.00 C ATOM 2021 O VAL A 1103 5.362 −9.265 −17.842 1.00 1.00 O ATOM 2022 CB VAL A 1103 6.441 −6.547 −18.503 1.00 1.00 C ATOM 2023 CG1 VAL A 1103 7.538 −5.652 −17.852 1.00 1.00 C ATOM 2024 CG2 VAL A 1103 5.828 −5.807 −19.745 1.00 1.00 C ATOM 2025 HA VAL A 1103 4.640 −6.127 −17.468 1.00 1.00 H ATOM 2026 HB VAL A 1103 7.007 −7.448 −18.815 1.00 1.00 H ATOM 2027 HG11 VAL A 1103 8.044 −6.139 −16.994 1.00 1.00 H ATOM 2028 HG12 VAL A 1103 8.345 −5.577 −18.662 1.00 1.00 H ATOM 2029 HG13 VAL A 1103 7.202 −4.633 −17.574 1.00 1.00 H ATOM 2030 HG21 VAL A 1103 5.518 −4.791 −19.489 1.00 1.00 H ATOM 2031 HG22 VAL A 1103 6.579 −5.695 −20.499 1.00 1.00 H ATOM 2032 HG23 VAL A 1103 4.967 −6.347 −20.143 1.00 1.00 H ATOM 2033 HN VAL A 1103 6.308 −8.016 −15.894 1.00 1.00 H ATOM 2034 N GLY A 1104 3.316 −8.171 −18.274 1.00 1.00 N ATOM 2035 CA GLY A 1104 2.623 −9.405 −18.555 1.00 1.00 C ATOM 2036 C GLY A 1104 1.494 −9.336 −19.560 1.00 1.00 C ATOM 2037 O GLY A 1104 1.287 −8.270 −20.132 1.00 1.00 O ATOM 2038 HA2 GLY A 1104 2.108 −9.666 −17.612 1.00 1.00 H ATOM 2039 HA1 GLY A 1104 3.350 −10.202 −18.649 1.00 1.00 H ATOM 2040 HN GLY A 1104 2.811 −7.350 −18.379 1.00 1.00 H ATOM 2041 N SER A 1105 0.740 −10.471 −19.715 1.00 1.00 N ATOM 2042 CA SER A 1105 −0.428 −10.562 −20.573 1.00 1.00 C ATOM 2043 C SER A 1105 −0.081 −11.052 −21.934 1.00 1.00 C ATOM 2044 O SER A 1105 0.900 −10.626 −22.551 1.00 1.00 O ATOM 2045 CB SER A 1105 −1.165 −9.239 −20.825 1.00 1.00 C ATOM 2046 OG SER A 1105 −2.512 −9.361 −21.310 1.00 1.00 O ATOM 2047 HA SER A 1105 −1.161 −11.250 −20.130 1.00 1.00 H ATOM 2048 HB1 SER A 1105 −0.675 −8.574 −21.603 1.00 1.00 H ATOM 2049 HB2 SER A 1105 −1.138 −8.677 −19.920 1.00 1.00 H ATOM 2050 HG SER A 1105 −3.048 −9.856 −20.708 1.00 1.00 H ATOM 2051 HN SER A 1105 0.947 −11.329 −19.170 1.00 1.00 H ATOM 2052 N SER A 1106 −0.906 −11.991 −22.459 1.00 1.00 N ATOM 2053 CA SER A 1106 −0.613 −12.527 −23.801 1.00 1.00 C ATOM 2054 C SER A 1106 0.755 −13.156 −23.889 1.00 1.00 C ATOM 2055 O SER A 1106 1.721 −12.531 −24.311 1.00 1.00 O ATOM 2056 CB SER A 1106 −0.811 −11.453 −24.904 1.00 1.00 C ATOM 2057 OG SER A 1106 −0.531 −11.976 −26.238 1.00 1.00 O ATOM 2058 HA SER A 1106 −1.293 −13.330 −24.064 1.00 1.00 H ATOM 2059 HB1 SER A 1106 −0.206 −10.577 −24.705 1.00 1.00 H ATOM 2060 HB2 SER A 1106 −1.882 −11.053 −24.886 1.00 1.00 H ATOM 2061 HG SER A 1106 0.399 −11.980 −26.374 1.00 1.00 H ATOM 2062 HN SER A 1106 −1.677 −12.383 −21.914 1.00 1.00 H ATOM 2063 N GLY A 1107 0.834 −14.467 −23.457 1.00 1.00 N ATOM 2064 CA GLY A 1107 2.148 −15.200 −23.460 1.00 1.00 C ATOM 2065 C GLY A 1107 2.868 −15.166 −22.152 1.00 1.00 C ATOM 2066 O GLY A 1107 3.780 −14.350 −22.076 1.00 1.00 O ATOM 2067 HA2 GLY A 1107 2.893 −14.810 −24.169 1.00 1.00 H ATOM 2068 HA1 GLY A 1107 1.921 −16.239 −23.777 1.00 1.00 H ATOM 2069 HN GLY A 1107 −0.009 −14.964 −23.187 1.00 1.00 H ATOM 2070 N LEU A 1108 2.642 −16.087 −21.177 1.00 1.00 N ATOM 2071 CA LEU A 1108 3.579 −16.164 −20.056 1.00 1.00 C ATOM 2072 C LEU A 1108 5.018 −16.420 −20.504 1.00 1.00 C ATOM 2073 O LEU A 1108 5.920 −15.749 −20.009 1.00 1.00 O ATOM 2074 CB LEU A 1108 3.175 −17.126 −18.938 1.00 1.00 C ATOM 2075 CG LEU A 1108 4.178 −17.250 −17.744 1.00 1.00 C ATOM 2076 CD1 LEU A 1108 4.582 −15.938 −17.124 1.00 1.00 C ATOM 2077 CD2 LEU A 1108 3.647 −18.262 −16.639 1.00 1.00 C ATOM 2078 HA LEU A 1108 3.584 −15.177 −19.627 1.00 1.00 H ATOM 2079 HB1 LEU A 1108 2.939 −18.151 −19.405 1.00 1.00 H ATOM 2080 HB2 LEU A 1108 2.171 −16.868 −18.569 1.00 1.00 H ATOM 2081 HG LEU A 1108 5.082 −17.775 −18.188 1.00 1.00 H ATOM 2082 HD21 LEU A 1108 4.419 −18.534 −15.870 1.00 1.00 H ATOM 2083 HD22 LEU A 1108 3.337 −19.173 −17.105 1.00 1.00 H ATOM 2084 HD23 LEU A 1108 2.773 −17.777 −16.140 1.00 1.00 H ATOM 2085 HD11 LEU A 1108 5.218 −15.347 −17.732 1.00 1.00 H ATOM 2086 HD12 LEU A 1108 5.079 −16.095 −16.169 1.00 1.00 H ATOM 2087 HD13 LEU A 1108 3.606 −15.346 −17.011 1.00 1.00 H ATOM 2088 HN LEU A 1108 1.880 −16.708 −21.231 1.00 1.00 H ATOM 2089 N SER A 1109 5.179 −17.447 −21.378 1.00 1.00 N ATOM 2090 CA SER A 1109 6.501 −17.943 −21.779 1.00 1.00 C ATOM 2091 C SER A 1109 7.471 −16.769 −22.032 1.00 1.00 C ATOM 2092 O SER A 1109 8.529 −16.663 −21.417 1.00 1.00 O ATOM 2093 CB SER A 1109 6.448 −18.887 −23.032 1.00 1.00 C ATOM 2094 OG SER A 1109 5.855 −18.239 −24.245 1.00 1.00 O ATOM 2095 HA SER A 1109 6.871 −18.496 −20.883 1.00 1.00 H ATOM 2096 HB1 SER A 1109 5.883 −19.834 −22.877 1.00 1.00 H ATOM 2097 HB2 SER A 1109 7.516 −19.105 −23.232 1.00 1.00 H ATOM 2098 HG SER A 1109 4.902 −18.129 −24.201 1.00 1.00 H ATOM 2099 HN SER A 1109 4.389 −17.950 −21.734 1.00 1.00 H ATOM 2100 N ARG A 1110 7.044 −15.860 −22.938 1.00 1.00 N ATOM 2101 CA ARG A 1110 7.995 −14.781 −23.302 1.00 1.00 C ATOM 2102 C ARG A 1110 8.407 −13.958 −22.095 1.00 1.00 C ATOM 2103 O ARG A 1110 9.516 −13.495 −22.030 1.00 1.00 O ATOM 2104 CB ARG A 1110 7.449 −13.889 −24.446 1.00 1.00 C ATOM 2105 CG ARG A 1110 6.230 −13.004 −23.921 1.00 1.00 C ATOM 2106 CD ARG A 1110 5.392 −12.497 −25.161 1.00 1.00 C ATOM 2107 NE ARG A 1110 4.170 −11.868 −24.603 1.00 1.00 N ATOM 2108 CZ ARG A 1110 4.093 −10.624 −24.167 1.00 1.00 C ATOM 2109 NH1 ARG A 1110 5.108 −9.796 −24.145 1.00 1.00 N ATOM 2110 NH2 ARG A 1110 2.909 −10.249 −23.737 1.00 1.00 N ATOM 2111 HA ARG A 1110 8.906 −15.239 −23.622 1.00 1.00 H ATOM 2112 HB1 ARG A 1110 7.101 −14.509 −25.280 1.00 1.00 H ATOM 2113 HB2 ARG A 1110 8.292 −13.240 −24.783 1.00 1.00 H ATOM 2114 HG1 ARG A 1110 6.660 −12.177 −23.272 1.00 1.00 H ATOM 2115 HG2 ARG A 1110 5.619 −13.682 −23.244 1.00 1.00 H ATOM 2116 HD1 ARG A 1110 5.078 −13.396 −25.651 1.00 1.00 H ATOM 2117 HD2 ARG A 1110 6.059 −11.951 −25.810 1.00 1.00 H ATOM 2118 HE ARG A 1110 3.317 −12.385 −24.612 1.00 1.00 H ATOM 2119 HH12 ARG A 1110 5.000 −8.791 −23.750 1.00 1.00 H ATOM 2120 HH11 ARG A 1110 6.015 −10.113 −24.453 1.00 1.00 H ATOM 2121 HH22 ARG A 1110 2.759 −9.310 −23.318 1.00 1.00 H ATOM 2122 HH21 ARG A 1110 2.046 −10.875 −23.741 1.00 1.00 H ATOM 2123 HN ARG A 1110 6.157 −15.980 −23.374 1.00 1.00 H ATOM 2124 N TYR A 1111 7.555 −13.748 −21.089 1.00 1.00 N ATOM 2125 CA TYR A 1111 8.038 −13.153 −19.828 1.00 1.00 C ATOM 2126 C TYR A 1111 9.068 −13.981 −19.133 1.00 1.00 C ATOM 2127 O TYR A 1111 10.226 −13.596 −19.009 1.00 1.00 O ATOM 2128 CB TYR A 1111 6.902 −12.605 −18.931 1.00 1.00 C ATOM 2129 CG TYR A 1111 6.056 −11.608 −19.776 1.00 1.00 C ATOM 2130 CD1 TYR A 1111 6.563 −10.342 −20.080 1.00 1.00 C ATOM 2131 CD2 TYR A 1111 4.821 −11.960 −20.304 1.00 1.00 C ATOM 2132 CE1 TYR A 1111 5.824 −9.389 −20.773 1.00 1.00 C ATOM 2133 CE2 TYR A 1111 4.081 −11.041 −21.058 1.00 1.00 C ATOM 2134 CZ TYR A 1111 4.529 −9.704 −21.240 1.00 1.00 C ATOM 2135 OH TYR A 1111 3.712 −8.761 −21.876 1.00 1.00 O ATOM 2136 HA TYR A 1111 8.570 −12.216 −20.191 1.00 1.00 H ATOM 2137 HB2 TYR A 1111 7.301 −12.047 −18.068 1.00 1.00 H ATOM 2138 HB1 TYR A 1111 6.309 −13.431 −18.521 1.00 1.00 H ATOM 2139 HD2 TYR A 1111 4.470 −12.940 −20.140 1.00 1.00 H ATOM 2140 HE2 TYR A 1111 3.096 −11.327 −21.427 1.00 1.00 H ATOM 2141 HE1 TYR A 1111 6.315 −8.402 −21.048 1.00 1.00 H ATOM 2142 HD1 TYR A 1111 7.540 −10.111 −19.709 1.00 1.00 H ATOM 2143 HH TYR A 1111 3.720 −7.931 −21.402 1.00 1.00 H ATOM 2144 HN TYR A 1111 6.628 −14.092 −21.066 1.00 1.00 H ATOM 2145 N VAL A 1112 8.701 −15.177 −18.611 1.00 1.00 N ATOM 2146 CA VAL A 1112 9.717 −16.020 −17.993 1.00 1.00 C ATOM 2147 C VAL A 1112 10.992 −16.104 −18.848 1.00 1.00 C ATOM 2148 O VAL A 1112 12.054 −15.999 −18.248 1.00 1.00 O ATOM 2149 CB VAL A 1112 9.156 −17.435 −17.801 1.00 1.00 C ATOM 2150 CG1 VAL A 1112 10.312 −18.429 −17.378 1.00 1.00 C ATOM 2151 CG2 VAL A 1112 8.123 −17.507 −16.676 1.00 1.00 C ATOM 2152 HA VAL A 1112 9.983 −15.510 −17.031 1.00 1.00 H ATOM 2153 HB VAL A 1112 8.577 −17.756 −18.683 1.00 1.00 H ATOM 2154 HG11 VAL A 1112 10.849 −18.082 −16.535 1.00 1.00 H ATOM 2155 HG12 VAL A 1112 11.105 −18.560 −18.128 1.00 1.00 H ATOM 2156 HG13 VAL A 1112 9.874 −19.444 −17.214 1.00 1.00 H ATOM 2157 HG21 VAL A 1112 7.722 −18.567 −16.569 1.00 1.00 H ATOM 2158 HG22 VAL A 1112 7.246 −16.837 −16.920 1.00 1.00 H ATOM 2159 HG23 VAL A 1112 8.465 −17.273 −15.675 1.00 1.00 H ATOM 2160 HN VAL A 1112 7.748 −15.499 −18.677 1.00 1.00 H ATOM 2161 N ALA A 1113 10.940 −16.236 −20.181 1.00 1.00 N ATOM 2162 CA ALA A 1113 12.166 −16.325 −20.955 1.00 1.00 C ATOM 2163 C ALA A 1113 12.860 −14.997 −20.871 1.00 1.00 C ATOM 2164 O ALA A 1113 13.974 −14.960 −20.403 1.00 1.00 O ATOM 2165 CB ALA A 1113 11.911 −16.632 −22.443 1.00 1.00 C ATOM 2166 HA ALA A 1113 12.767 −17.170 −20.580 1.00 1.00 H ATOM 2167 HB1 ALA A 1113 11.445 −17.600 −22.574 1.00 1.00 H ATOM 2168 HB2 ALA A 1113 12.870 −16.646 −22.949 1.00 1.00 H ATOM 2169 HB3 ALA A 1113 11.323 −15.833 −22.943 1.00 1.00 H ATOM 2170 HN ALA A 1113 10.072 −16.239 −20.666 1.00 1.00 H ATOM 2171 N ARG A 1114 12.182 −13.881 −21.263 1.00 1.00 N ATOM 2172 CA ARG A 1114 12.948 −12.614 −21.359 1.00 1.00 C ATOM 2173 C ARG A 1114 12.991 −11.926 −19.975 1.00 1.00 C ATOM 2174 O ARG A 1114 14.084 −11.545 −19.498 1.00 1.00 O ATOM 2175 CB ARG A 1114 12.330 −11.664 −22.424 1.00 1.00 C ATOM 2176 CG ARG A 1114 13.245 −10.492 −22.948 1.00 1.00 C ATOM 2177 CD ARG A 1114 13.471 −9.370 −21.889 1.00 1.00 C ATOM 2178 NE ARG A 1114 14.445 −9.687 −20.798 1.00 1.00 N ATOM 2179 CZ ARG A 1114 14.593 −8.958 −19.715 1.00 1.00 C ATOM 2180 NH1 ARG A 1114 13.880 −7.902 −19.485 1.00 1.00 N ATOM 2181 NH2 ARG A 1114 15.479 −9.307 −18.836 1.00 1.00 N ATOM 2182 HA ARG A 1114 13.973 −12.832 −21.666 1.00 1.00 H ATOM 2183 HB1 ARG A 1114 11.332 −11.238 −22.114 1.00 1.00 H ATOM 2184 HB2 ARG A 1114 12.140 −12.314 −23.314 1.00 1.00 H ATOM 2185 HG1 ARG A 1114 12.702 −10.056 −23.810 1.00 1.00 H ATOM 2186 HG2 ARG A 1114 14.204 −10.823 −23.358 1.00 1.00 H ATOM 2187 HD1 ARG A 1114 12.503 −9.216 −21.478 1.00 1.00 H ATOM 2188 HD2 ARG A 1114 13.802 −8.449 −22.363 1.00 1.00 H ATOM 2189 HE ARG A 1114 15.051 −10.516 −20.947 1.00 1.00 H ATOM 2190 HH12 ARG A 1114 14.015 −7.327 −18.666 1.00 1.00 H ATOM 2191 HH11 ARG A 1114 13.216 −7.533 −20.173 1.00 1.00 H ATOM 2192 HH22 ARG A 1114 15.676 −8.762 −17.943 1.00 1.00 H ATOM 2193 HH21 ARG A 1114 16.040 −10.167 −18.981 1.00 1.00 H ATOM 2194 HN ARG A 1114 11.119 −13.932 −21.488 1.00 1.00 H ATOM 2195 N LEU A 1115 11.821 −11.619 −19.393 1.00 1.00 N ATOM 2196 CA LEU A 1115 11.791 −10.973 −18.095 1.00 1.00 C ATOM 2197 C LEU A 1115 12.716 −11.707 −17.199 1.00 1.00 C ATOM 2198 O LEU A 1115 13.669 −11.099 −16.724 1.00 1.00 O ATOM 2199 CB LEU A 1115 10.307 −10.820 −17.573 1.00 1.00 C ATOM 2200 CG LEU A 1115 10.056 −9.883 −16.340 1.00 1.00 C ATOM 2201 CD1 LEU A 1115 8.559 −9.887 −15.942 1.00 1.00 C ATOM 2202 CD2 LEU A 1115 11.051 −10.146 −15.166 1.00 1.00 C ATOM 2203 HA LEU A 1115 12.199 −9.971 −18.211 1.00 1.00 H ATOM 2204 HB1 LEU A 1115 9.883 −11.795 −17.215 1.00 1.00 H ATOM 2205 HB2 LEU A 1115 9.681 −10.484 −18.410 1.00 1.00 H ATOM 2206 HG LEU A 1115 10.226 −8.888 −16.763 1.00 1.00 H ATOM 2207 HD21 LEU A 1115 10.956 −11.208 −14.821 1.00 1.00 H ATOM 2208 HD22 LEU A 1115 10.743 −9.426 −14.365 1.00 1.00 H ATOM 2209 HD23 LEU A 1115 12.070 −9.887 −15.549 1.00 1.00 H ATOM 2210 HD11 LEU A 1115 7.957 −9.575 −16.772 1.00 1.00 H ATOM 2211 HD12 LEU A 1115 8.386 −9.201 −15.147 1.00 1.00 H ATOM 2212 HD13 LEU A 1115 8.259 −10.863 −15.687 1.00 1.00 H ATOM 2213 HN LEU A 1115 10.953 −11.945 −19.801 1.00 1.00 H ATOM 2214 N SER A 1116 12.399 −12.986 −16.952 1.00 1.00 N ATOM 2215 CA SER A 1116 13.301 −13.796 −16.107 1.00 1.00 C ATOM 2216 C SER A 1116 13.378 −13.340 −14.652 1.00 1.00 C ATOM 2217 O SER A 1116 13.013 −14.133 −13.812 1.00 1.00 O ATOM 2218 CB SER A 1116 14.693 −13.945 −16.796 1.00 1.00 C ATOM 2219 OG SER A 1116 15.553 −14.621 −15.875 1.00 1.00 O ATOM 2220 HA SER A 1116 12.907 −14.783 −16.124 1.00 1.00 H ATOM 2221 HB1 SER A 1116 15.058 −12.965 −17.172 1.00 1.00 H ATOM 2222 HB2 SER A 1116 14.656 −14.554 −17.749 1.00 1.00 H ATOM 2223 HG SER A 1116 16.378 −14.895 −16.258 1.00 1.00 H ATOM 2224 HN SER A 1116 11.688 −13.529 −17.462 1.00 1.00 H ATOM 2225 N SER A 1117 13.875 −12.127 −14.340 1.00 1.00 N ATOM 2226 CA SER A 1117 14.086 −11.818 −12.916 1.00 1.00 C ATOM 2227 C SER A 1117 12.878 −12.071 −12.004 1.00 1.00 C ATOM 2228 O SER A 1117 11.768 −12.035 −12.498 1.00 1.00 O ATOM 2229 CB SER A 1117 14.374 −10.313 −12.747 1.00 1.00 C ATOM 2230 OG SER A 1117 15.665 −9.951 −13.181 1.00 1.00 O ATOM 2231 HA SER A 1117 14.964 −12.389 −12.607 1.00 1.00 H ATOM 2232 HB1 SER A 1117 14.480 −9.997 −11.698 1.00 1.00 H ATOM 2233 HB2 SER A 1117 13.572 −9.683 −13.183 1.00 1.00 H ATOM 2234 HG SER A 1117 15.864 −10.036 −14.098 1.00 1.00 H ATOM 2235 HN SER A 1117 14.194 −11.494 −15.029 1.00 1.00 H ATOM 2236 N ASN A 1118 13.159 −12.257 −10.673 1.00 1.00 N ATOM 2237 CA ASN A 1118 12.121 −12.657 −9.756 1.00 1.00 C ATOM 2238 C ASN A 1118 10.729 −12.067 −9.978 1.00 1.00 C ATOM 2239 O ASN A 1118 9.806 −12.791 −9.646 1.00 1.00 O ATOM 2240 CB ASN A 1118 12.485 −12.443 −8.304 1.00 1.00 C ATOM 2241 CG ASN A 1118 12.656 −10.989 −7.978 1.00 1.00 C ATOM 2242 OD1 ASN A 1118 12.407 −10.138 −8.819 1.00 1.00 O ATOM 2243 ND2 ASN A 1118 13.114 −10.551 −6.763 1.00 1.00 N ATOM 2244 HA ASN A 1118 11.900 −13.683 −9.986 1.00 1.00 H ATOM 2245 HB1 ASN A 1118 13.392 −13.002 −8.069 1.00 1.00 H ATOM 2246 HB2 ASN A 1118 11.715 −12.824 −7.590 1.00 1.00 H ATOM 2247 HD22 ASN A 1118 13.219 −9.591 −6.655 1.00 1.00 H ATOM 2248 HD21 ASN A 1118 13.372 −11.224 −6.006 1.00 1.00 H ATOM 2249 HN ASN A 1118 14.136 −12.225 −10.365 1.00 1.00 H ATOM 2250 N SER A 1119 10.457 −10.877 −10.569 1.00 1.00 N ATOM 2251 CA SER A 1119 9.074 −10.434 −10.770 1.00 1.00 C ATOM 2252 C SER A 1119 8.265 −11.387 −11.632 1.00 1.00 C ATOM 2253 O SER A 1119 7.056 −11.316 −11.545 1.00 1.00 O ATOM 2254 CB SER A 1119 9.053 −9.048 −11.522 1.00 1.00 C ATOM 2255 OG SER A 1119 7.671 −8.656 −11.694 1.00 1.00 O ATOM 2256 HA SER A 1119 8.527 −10.322 −9.830 1.00 1.00 H ATOM 2257 HB1 SER A 1119 9.443 −9.205 −12.518 1.00 1.00 H ATOM 2258 HB2 SER A 1119 9.691 −8.258 −11.061 1.00 1.00 H ATOM 2259 HG SER A 1119 7.267 −8.499 −10.856 1.00 1.00 H ATOM 2260 HN SER A 1119 11.215 −10.305 −10.875 1.00 1.00 H ATOM 2261 N ARG A 1120 8.865 −12.256 −12.515 1.00 1.00 N ATOM 2262 CA ARG A 1120 8.014 −13.116 −13.357 1.00 1.00 C ATOM 2263 C ARG A 1120 6.892 −13.792 −12.624 1.00 1.00 C ATOM 2264 O ARG A 1120 7.007 −14.146 −11.455 1.00 1.00 O ATOM 2265 CB ARG A 1120 8.854 −14.165 −14.136 1.00 1.00 C ATOM 2266 CG ARG A 1120 9.314 −15.449 −13.367 1.00 1.00 C ATOM 2267 CD ARG A 1120 10.091 −15.121 −12.033 1.00 1.00 C ATOM 2268 NE ARG A 1120 10.572 −16.404 −11.473 1.00 1.00 N ATOM 2269 CZ ARG A 1120 11.729 −16.974 −11.769 1.00 1.00 C ATOM 2270 NH1 ARG A 1120 12.566 −16.469 −12.619 1.00 1.00 N ATOM 2271 NH2 ARG A 1120 12.029 −18.057 −11.137 1.00 1.00 N ATOM 2272 HA ARG A 1120 7.641 −12.344 −14.041 1.00 1.00 H ATOM 2273 HB1 ARG A 1120 9.757 −13.615 −14.518 1.00 1.00 H ATOM 2274 HB2 ARG A 1120 8.277 −14.473 −15.047 1.00 1.00 H ATOM 2275 HG1 ARG A 1120 9.962 −16.051 −13.976 1.00 1.00 H ATOM 2276 HG2 ARG A 1120 8.393 −16.029 −13.193 1.00 1.00 H ATOM 2277 HD1 ARG A 1120 9.432 −14.680 −11.317 1.00 1.00 H ATOM 2278 HD2 ARG A 1120 10.855 −14.342 −12.157 1.00 1.00 H ATOM 2279 HE ARG A 1120 9.967 −16.856 −10.760 1.00 1.00 H ATOM 2280 HH12 ARG A 1120 13.469 −16.899 −12.829 1.00 1.00 H ATOM 2281 HH11 ARG A 1120 12.343 −15.631 −13.199 1.00 1.00 H ATOM 2282 HH22 ARG A 1120 12.919 −18.532 −11.328 1.00 1.00 H ATOM 2283 HH21 ARG A 1120 11.387 −18.547 −10.442 1.00 1.00 H ATOM 2284 HN ARG A 1120 9.867 −12.216 −12.572 1.00 1.00 H ATOM 2285 N ILE A 1121 5.726 −13.981 −13.292 1.00 1.00 N ATOM 2286 CA ILE A 1121 4.513 −14.349 −12.540 1.00 1.00 C ATOM 2287 C ILE A 1121 3.355 −14.670 −13.476 1.00 1.00 C ATOM 2288 O ILE A 1121 3.224 −13.933 −14.460 1.00 1.00 O ATOM 2289 CB ILE A 1121 4.019 −13.329 −11.469 1.00 1.00 C ATOM 2290 CG1 ILE A 1121 2.729 −13.813 −10.707 1.00 1.00 C ATOM 2291 CG2 ILE A 1121 3.787 −11.999 −12.193 1.00 1.00 C ATOM 2292 CD1 ILE A 1121 2.213 −12.810 −9.698 1.00 1.00 C ATOM 2293 HA ILE A 1121 4.697 −15.317 −12.001 1.00 1.00 H ATOM 2294 HB ILE A 1121 4.769 −13.174 −10.681 1.00 1.00 H ATOM 2295 HG11 ILE A 1121 2.922 −14.841 −10.321 1.00 1.00 H ATOM 2296 HG12 ILE A 1121 1.892 −13.887 −11.419 1.00 1.00 H ATOM 2297 HD11 ILE A 1121 1.817 −11.934 −10.216 1.00 1.00 H ATOM 2298 HD12 ILE A 1121 3.011 −12.583 −8.984 1.00 1.00 H ATOM 2299 HD13 ILE A 1121 1.332 −13.183 −9.133 1.00 1.00 H ATOM 2300 HG21 ILE A 1121 3.575 −11.166 −11.536 1.00 1.00 H ATOM 2301 HG22 ILE A 1121 2.970 −12.028 −12.961 1.00 1.00 H ATOM 2302 HG23 ILE A 1121 4.708 −11.723 −12.674 1.00 1.00 H ATOM 2303 HN ILE A 1121 5.604 −13.713 −14.260 1.00 1.00 H ATOM 2304 N PHE A 1122 2.523 −15.677 −13.227 1.00 1.00 N ATOM 2305 CA PHE A 1122 1.317 −15.919 −14.087 1.00 1.00 C ATOM 2306 C PHE A 1122 0.289 −14.817 −13.921 1.00 1.00 C ATOM 2307 O PHE A 1122 −0.762 −15.093 −13.338 1.00 1.00 O ATOM 2308 CB PHE A 1122 0.718 −17.315 −13.781 1.00 1.00 C ATOM 2309 CG PHE A 1122 −0.476 −17.728 −14.695 1.00 1.00 C ATOM 2310 CD1 PHE A 1122 −0.333 −17.850 −16.067 1.00 1.00 C ATOM 2311 CD2 PHE A 1122 −1.730 −17.988 −14.133 1.00 1.00 C ATOM 2312 CE1 PHE A 1122 −1.390 −18.311 −16.881 1.00 1.00 C ATOM 2313 CE2 PHE A 1122 −2.824 −18.391 −14.913 1.00 1.00 C ATOM 2314 CZ PHE A 1122 −2.625 −18.551 −16.279 1.00 1.00 C ATOM 2315 HA PHE A 1122 1.591 −15.911 −15.178 1.00 1.00 H ATOM 2316 HB1 PHE A 1122 0.420 −17.262 −12.718 1.00 1.00 H ATOM 2317 HB2 PHE A 1122 1.473 −18.112 −13.905 1.00 1.00 H ATOM 2318 HD2 PHE A 1122 −1.846 −17.893 −13.035 1.00 1.00 H ATOM 2319 HE2 PHE A 1122 −3.833 −18.502 −14.510 1.00 1.00 H ATOM 2320 HZ PHE A 1122 −3.448 −18.913 −16.874 1.00 1.00 H ATOM 2321 HE1 PHE A 1122 −1.259 −18.447 −17.909 1.00 1.00 H ATOM 2322 HD1 PHE A 1122 0.589 −17.613 −16.654 1.00 1.00 H ATOM 2323 HN PHE A 1122 2.639 −16.283 −12.442 1.00 1.00 H ATOM 2324 N ASN A 1123 0.583 −13.611 −14.413 1.00 1.00 N ATOM 2325 CA ASN A 1123 −0.403 −12.495 −14.218 1.00 1.00 C ATOM 2326 C ASN A 1123 −0.998 −11.957 −15.526 1.00 1.00 C ATOM 2327 O ASN A 1123 −0.263 −11.994 −16.515 1.00 1.00 O ATOM 2328 CB ASN A 1123 0.145 −11.269 −13.429 1.00 1.00 C ATOM 2329 CG ASN A 1123 −0.872 −10.367 −12.817 1.00 1.00 C ATOM 2330 OD1 ASN A 1123 −2.037 −10.604 −12.887 1.00 1.00 O ATOM 2331 ND2 ASN A 1123 −0.476 −9.222 −12.222 1.00 1.00 N ATOM 2332 HA ASN A 1123 −1.280 −12.773 −13.584 1.00 1.00 H ATOM 2333 HB1 ASN A 1123 0.904 −10.736 −14.032 1.00 1.00 H ATOM 2334 HB2 ASN A 1123 0.641 −11.744 −12.616 1.00 1.00 H ATOM 2335 HD22 ASN A 1123 −1.210 −8.547 −11.997 1.00 1.00 H ATOM 2336 HD21 ASN A 1123 0.466 −8.978 −11.987 1.00 1.00 H ATOM 2337 HN ASN A 1123 1.419 −13.479 −14.959 1.00 1.00 H ATOM 2338 N TYR A 1124 −2.215 −11.410 −15.516 1.00 1.00 N ATOM 2339 CA TYR A 1124 −2.912 −10.891 −16.737 1.00 1.00 C ATOM 2340 C TYR A 1124 −2.972 −11.906 −17.875 1.00 1.00 C ATOM 2341 O TYR A 1124 −3.485 −11.480 −18.900 1.00 1.00 O ATOM 2342 CB TYR A 1124 −2.153 −9.635 −17.176 1.00 1.00 C ATOM 2343 CG TYR A 1124 −1.938 −8.590 −16.088 1.00 1.00 C ATOM 2344 CD1 TYR A 1124 −2.957 −8.112 −15.279 1.00 1.00 C ATOM 2345 CD2 TYR A 1124 −0.662 −8.093 −15.817 1.00 1.00 C ATOM 2346 CE1 TYR A 1124 −2.716 −7.111 −14.336 1.00 1.00 C ATOM 2347 CE2 TYR A 1124 −0.357 −7.199 −14.777 1.00 1.00 C ATOM 2348 CZ TYR A 1124 −1.424 −6.768 −13.947 1.00 1.00 C ATOM 2349 OH TYR A 1124 −1.271 −5.956 −12.806 1.00 1.00 O ATOM 2350 HA TYR A 1124 −3.956 −10.598 −16.581 1.00 1.00 H ATOM 2351 HB2 TYR A 1124 −2.774 −9.118 −17.906 1.00 1.00 H ATOM 2352 HB1 TYR A 1124 −1.221 −9.950 −17.650 1.00 1.00 H ATOM 2353 HD2 TYR A 1124 0.108 −8.362 −16.535 1.00 1.00 H ATOM 2354 HE2 TYR A 1124 0.633 −6.859 −14.657 1.00 1.00 H ATOM 2355 HE1 TYR A 1124 −3.580 −6.578 −13.955 1.00 1.00 H ATOM 2356 HD1 TYR A 1124 −3.978 −8.461 −15.384 1.00 1.00 H ATOM 2357 HH TYR A 1124 −0.422 −5.564 −12.720 1.00 1.00 H ATOM 2358 HN TYR A 1124 −2.621 −11.229 −14.643 1.00 1.00 H ATOM 2359 N GLN A 1125 −2.555 −13.175 −17.808 1.00 1.00 N ATOM 2360 CA GLN A 1125 −3.026 −14.086 −18.876 1.00 1.00 C ATOM 2361 C GLN A 1125 −4.521 −14.185 −18.742 1.00 1.00 C ATOM 2362 O GLN A 1125 −4.864 −14.867 −17.797 1.00 1.00 O ATOM 2363 CB GLN A 1125 −2.379 −15.510 −18.785 1.00 1.00 C ATOM 2364 CG GLN A 1125 −0.989 −15.592 −19.456 1.00 1.00 C ATOM 2365 CD GLN A 1125 −0.138 −14.394 −19.061 1.00 1.00 C ATOM 2366 OE1 GLN A 1125 0.283 −13.593 −19.875 1.00 1.00 O ATOM 2367 NE2 GLN A 1125 0.132 −14.238 −17.773 1.00 1.00 N ATOM 2368 HA GLN A 1125 −2.724 −13.610 −19.844 1.00 1.00 H ATOM 2369 HB1 GLN A 1125 −3.026 −16.335 −19.150 1.00 1.00 H ATOM 2370 HB2 GLN A 1125 −2.279 −15.746 −17.716 1.00 1.00 H ATOM 2371 HG1 GLN A 1125 −1.051 −15.620 −20.552 1.00 1.00 H ATOM 2372 HG2 GLN A 1125 −0.424 −16.454 −19.083 1.00 1.00 H ATOM 2373 HE22 GLN A 1125 0.760 −13.504 −17.446 1.00 1.00 H ATOM 2374 HE21 GLN A 1125 −0.122 −14.869 −17.072 1.00 1.00 H ATOM 2375 HN GLN A 1125 −2.129 −13.513 −16.988 1.00 1.00 H ATOM 2376 N HIS A 1126 −5.355 −13.533 −19.565 1.00 1.00 N ATOM 2377 CA HIS A 1126 −6.765 −13.570 −19.303 1.00 1.00 C ATOM 2378 C HIS A 1126 −7.556 −13.546 −20.569 1.00 1.00 C ATOM 2379 O HIS A 1126 −6.914 −13.482 −21.623 1.00 1.00 O ATOM 2380 CB HIS A 1126 −7.080 −12.456 −18.280 1.00 1.00 C ATOM 2381 CG HIS A 1126 −7.202 −11.063 −18.956 1.00 1.00 C ATOM 2382 ND1 HIS A 1126 −6.166 −10.441 −19.455 1.00 1.00 N ATOM 2383 CD2 HIS A 1126 −8.329 −10.294 −19.019 1.00 1.00 C ATOM 2384 CE1 HIS A 1126 −6.548 −9.279 −19.848 1.00 1.00 C ATOM 2385 NE2 HIS A 1126 −7.781 −9.120 −19.629 1.00 1.00 N ATOM 2386 HA HIS A 1126 −7.018 −14.545 −18.918 1.00 1.00 H ATOM 2387 HB1 HIS A 1126 −6.278 −12.316 −17.537 1.00 1.00 H ATOM 2388 HB2 HIS A 1126 −8.052 −12.708 −17.805 1.00 1.00 H ATOM 2389 HD2 HIS A 1126 −9.376 −10.455 −18.647 1.00 1.00 H ATOM 2390 HE1 HIS A 1126 −5.979 −8.501 −20.367 1.00 1.00 H ATOM 2391 HD1 HIS A 1126 −5.216 −10.784 −19.515 1.00 1.00 H ATOM 2392 HN HIS A 1126 −5.036 −13.026 −20.428 1.00 1.00 H ATOM 2393 N GLY A 1127 −8.898 −13.496 −20.516 1.00 1.00 N ATOM 2394 CA GLY A 1127 −9.668 −13.355 −21.767 1.00 1.00 C ATOM 2395 C GLY A 1127 −10.237 −11.998 −21.944 1.00 1.00 C ATOM 2396 O GLY A 1127 −11.465 −11.858 −21.993 1.00 1.00 O ATOM 2397 HA2 GLY A 1127 −10.460 −14.094 −21.701 1.00 1.00 H ATOM 2398 HA1 GLY A 1127 −9.020 −13.607 −22.640 1.00 1.00 H ATOM 2399 HN GLY A 1127 −9.347 −13.632 −19.630 1.00 1.00 H ATOM 2400 N THR A 1128 −9.443 −10.895 −22.071 1.00 1.00 N ATOM 2401 CA THR A 1128 −9.879 −9.477 −22.130 1.00 1.00 C ATOM 2402 C THR A 1128 −10.967 −8.972 −21.152 1.00 1.00 C ATOM 2403 O THR A 1128 −10.816 −7.951 −20.500 1.00 1.00 O ATOM 2404 CB THR A 1128 −10.195 −8.961 −23.559 1.00 1.00 C ATOM 2405 OG1 THR A 1128 −10.607 −7.557 −23.529 1.00 1.00 O ATOM 2406 CG2 THR A 1128 −11.136 −9.840 −24.374 1.00 1.00 C ATOM 2407 HA THR A 1128 −9.023 −8.846 −21.812 1.00 1.00 H ATOM 2408 HB THR A 1128 −9.248 −9.002 −24.138 1.00 1.00 H ATOM 2409 HG1 THR A 1128 −11.496 −7.480 −23.184 1.00 1.00 H ATOM 2410 HG23 THR A 1128 −11.298 −9.363 −25.332 1.00 1.00 H ATOM 2411 HG21 THR A 1128 −12.111 −9.822 −23.850 1.00 1.00 H ATOM 2412 HG22 THR A 1128 −10.734 −10.841 −24.417 1.00 1.00 H ATOM 2413 HN THR A 1128 −8.454 −11.063 −22.019 1.00 1.00 H ATOM 2414 N MET A 1129 −12.191 −9.636 −21.119 1.00 1.00 N ATOM 2415 CA MET A 1129 −13.340 −9.053 −20.366 1.00 1.00 C ATOM 2416 C MET A 1129 −13.954 −7.964 −21.239 1.00 1.00 C ATOM 2417 O MET A 1129 −15.008 −8.202 −21.817 1.00 1.00 O ATOM 2418 CB MET A 1129 −14.447 −10.107 −20.004 1.00 1.00 C ATOM 2419 CG MET A 1129 −13.827 −11.324 −19.258 1.00 1.00 C ATOM 2420 SD MET A 1129 −15.064 −12.387 −18.482 1.00 1.00 S ATOM 2421 CE MET A 1129 −15.552 −13.170 −20.078 1.00 1.00 C ATOM 2422 HA MET A 1129 −12.983 −8.545 −19.465 1.00 1.00 H ATOM 2423 HB1 MET A 1129 −14.990 −10.467 −20.914 1.00 1.00 H ATOM 2424 HB2 MET A 1129 −15.158 −9.608 −19.327 1.00 1.00 H ATOM 2425 HG1 MET A 1129 −13.263 −10.919 −18.451 1.00 1.00 H ATOM 2426 HG2 MET A 1129 −13.149 −11.860 −19.909 1.00 1.00 H ATOM 2427 HE1 MET A 1129 −16.049 −12.422 −20.629 1.00 1.00 H ATOM 2428 HE2 MET A 1129 −16.314 −13.940 −19.906 1.00 1.00 H ATOM 2429 HE3 MET A 1129 −14.690 −13.602 −20.612 1.00 1.00 H ATOM 2430 HN MET A 1129 −12.379 −10.471 −21.628 1.00 1.00 H ATOM 2431 N GLN A 1130 −13.316 −6.777 −21.352 1.00 1.00 N ATOM 2432 CA GLN A 1130 −13.896 −5.700 −22.115 1.00 1.00 C ATOM 2433 C GLN A 1130 −12.820 −4.694 −22.434 1.00 1.00 C ATOM 2434 O GLN A 1130 −11.947 −4.537 −21.601 1.00 1.00 O ATOM 2435 CB GLN A 1130 −15.108 −5.124 −21.354 1.00 1.00 C ATOM 2436 CG GLN A 1130 −15.947 −4.150 −22.251 1.00 1.00 C ATOM 2437 CD GLN A 1130 −16.265 −4.686 −23.651 1.00 1.00 C ATOM 2438 OE1 GLN A 1130 −16.203 −3.930 −24.590 1.00 1.00 O ATOM 2439 NE2 GLN A 1130 −16.587 −5.989 −23.917 1.00 1.00 N ATOM 2440 HA GLN A 1130 −14.171 −6.163 −23.079 1.00 1.00 H ATOM 2441 HB1 GLN A 1130 −14.743 −4.629 −20.387 1.00 1.00 H ATOM 2442 HB2 GLN A 1130 −15.755 −5.951 −21.029 1.00 1.00 H ATOM 2443 HG1 GLN A 1130 −15.399 −3.220 −22.409 1.00 1.00 H ATOM 2444 HG2 GLN A 1130 −16.856 −3.773 −21.761 1.00 1.00 H ATOM 2445 HE22 GLN A 1130 −16.714 −6.359 −24.849 1.00 1.00 H ATOM 2446 HE21 GLN A 1130 −16.659 −6.665 −23.144 1.00 1.00 H ATOM 2447 HN GLN A 1130 −12.436 −6.641 −20.891 1.00 1.00 H ATOM 2448 N ASN A 1131 −12.861 −4.077 −23.637 1.00 1.00 N ATOM 2449 CA ASN A 1131 −11.774 −3.125 −24.022 1.00 1.00 C ATOM 2450 C ASN A 1131 −11.143 −2.310 −22.889 1.00 1.00 C ATOM 2451 O ASN A 1131 −9.935 −2.368 −22.730 1.00 1.00 O ATOM 2452 CB ASN A 1131 −10.723 −3.897 −24.819 1.00 1.00 C ATOM 2453 CG ASN A 1131 −11.461 −4.622 −25.897 1.00 1.00 C ATOM 2454 OD1 ASN A 1131 −12.002 −3.971 −26.758 1.00 1.00 O ATOM 2455 ND2 ASN A 1131 −11.536 −5.968 −25.938 1.00 1.00 N ATOM 2456 HA ASN A 1131 −12.229 −2.370 −24.621 1.00 1.00 H ATOM 2457 HB1 ASN A 1131 −10.216 −4.616 −24.196 1.00 1.00 H ATOM 2458 HB2 ASN A 1131 −9.908 −3.327 −25.272 1.00 1.00 H ATOM 2459 HD22 ASN A 1131 −11.966 −6.412 −26.693 1.00 1.00 H ATOM 2460 HD21 ASN A 1131 −11.144 −6.582 −25.221 1.00 1.00 H ATOM 2461 HN ASN A 1131 −13.585 −4.260 −24.345 1.00 1.00 H ATOM 2462 N LEU A 1132 −12.023 −1.631 −22.086 1.00 1.00 N ATOM 2463 CA LEU A 1132 −11.514 −1.000 −20.872 1.00 1.00 C ATOM 2464 C LEU A 1132 −10.592 −1.923 −20.097 1.00 1.00 C ATOM 2465 O LEU A 1132 −9.443 −1.581 −19.943 1.00 1.00 O ATOM 2466 CB LEU A 1132 −12.627 −0.375 −19.965 1.00 1.00 C ATOM 2467 CG LEU A 1132 −12.323 0.858 −19.081 1.00 1.00 C ATOM 2468 CD1 LEU A 1132 −13.620 1.318 −18.335 1.00 1.00 C ATOM 2469 CD2 LEU A 1132 −11.117 0.659 −18.126 1.00 1.00 C ATOM 2470 HA LEU A 1132 −10.976 −0.094 −21.212 1.00 1.00 H ATOM 2471 HB1 LEU A 1132 −13.055 −1.152 −19.346 1.00 1.00 H ATOM 2472 HB2 LEU A 1132 −13.467 −0.043 −20.649 1.00 1.00 H ATOM 2473 HG LEU A 1132 −12.020 1.694 −19.677 1.00 1.00 H ATOM 2474 HD21 LEU A 1132 −11.341 −0.320 −17.621 1.00 1.00 H ATOM 2475 HD22 LEU A 1132 −10.920 1.421 −17.367 1.00 1.00 H ATOM 2476 HD23 LEU A 1132 −10.192 0.476 −18.718 1.00 1.00 H ATOM 2477 HD11 LEU A 1132 −14.093 0.452 −17.796 1.00 1.00 H ATOM 2478 HD12 LEU A 1132 −14.380 1.708 −19.043 1.00 1.00 H ATOM 2479 HD13 LEU A 1132 −13.357 2.113 −17.578 1.00 1.00 H ATOM 2480 HN LEU A 1132 −13.023 −1.690 −22.239 1.00 1.00 H ATOM 2481 N HIS A 1133 −11.044 −3.094 −19.593 1.00 1.00 N ATOM 2482 CA HIS A 1133 −10.145 −3.881 −18.744 1.00 1.00 C ATOM 2483 C HIS A 1133 −8.786 −4.227 −19.329 1.00 1.00 C ATOM 2484 O HIS A 1133 −7.773 −4.078 −18.649 1.00 1.00 O ATOM 2485 CB HIS A 1133 −10.796 −5.206 −18.318 1.00 1.00 C ATOM 2486 CG HIS A 1133 −9.812 −6.050 −17.522 1.00 1.00 C ATOM 2487 ND1 HIS A 1133 −8.852 −6.788 −18.045 1.00 1.00 N ATOM 2488 CD2 HIS A 1133 −9.788 −6.128 −16.183 1.00 1.00 C ATOM 2489 CE1 HIS A 1133 −8.154 −7.331 −17.095 1.00 1.00 C ATOM 2490 NE2 HIS A 1133 −8.660 −6.955 −15.993 1.00 1.00 N ATOM 2491 HA HIS A 1133 −9.963 −3.300 −17.867 1.00 1.00 H ATOM 2492 HB1 HIS A 1133 −11.092 −5.762 −19.250 1.00 1.00 H ATOM 2493 HB2 HIS A 1133 −11.701 −5.122 −17.695 1.00 1.00 H ATOM 2494 HD2 HIS A 1133 −10.411 −5.689 −15.393 1.00 1.00 H ATOM 2495 HE1 HIS A 1133 −7.299 −7.968 −17.206 1.00 1.00 H ATOM 2496 HD1 HIS A 1133 −8.744 −6.984 −19.051 1.00 1.00 H ATOM 2497 HN HIS A 1133 −12.003 −3.457 −19.702 1.00 1.00 H ATOM 2498 N ASP A 1134 −8.750 −4.639 −20.615 1.00 1.00 N ATOM 2499 CA ASP A 1134 −7.421 −4.946 −21.196 1.00 1.00 C ATOM 2500 C ASP A 1134 −6.575 −3.656 −21.330 1.00 1.00 C ATOM 2501 O ASP A 1134 −5.377 −3.677 −21.118 1.00 1.00 O ATOM 2502 CB ASP A 1134 −7.599 −5.627 −22.575 1.00 1.00 C ATOM 2503 CG ASP A 1134 −6.322 −6.099 −23.228 1.00 1.00 C ATOM 2504 OD1 ASP A 1134 −5.650 −7.009 −22.629 1.00 1.00 O ATOM 2505 OD2 ASP A 1134 −5.934 −5.617 −24.324 1.00 1.00 O ATOM 2506 HA ASP A 1134 −6.910 −5.665 −20.546 1.00 1.00 H ATOM 2507 HB1 ASP A 1134 −8.037 −4.845 −23.237 1.00 1.00 H ATOM 2508 HB2 ASP A 1134 −8.251 −6.507 −22.430 1.00 1.00 H ATOM 2509 HN ASP A 1134 −9.624 −4.719 −21.187 1.00 1.00 H ATOM 2510 N SER A 1135 −7.168 −2.496 −21.662 1.00 1.00 N ATOM 2511 CA SER A 1135 −6.404 −1.246 −21.574 1.00 1.00 C ATOM 2512 C SER A 1135 −5.891 −1.091 −20.164 1.00 1.00 C ATOM 2513 O SER A 1135 −4.752 −0.673 −20.085 1.00 1.00 O ATOM 2514 CB SER A 1135 −7.279 −0.039 −22.006 1.00 1.00 C ATOM 2515 OG SER A 1135 −7.944 0.549 −20.907 1.00 1.00 O ATOM 2516 HA SER A 1135 −5.542 −1.329 −22.221 1.00 1.00 H ATOM 2517 HB1 SER A 1135 −7.889 −0.137 −22.924 1.00 1.00 H ATOM 2518 HB2 SER A 1135 −6.571 0.742 −22.346 1.00 1.00 H ATOM 2519 HG SER A 1135 −8.574 −0.043 −20.516 1.00 1.00 H ATOM 2520 HN SER A 1135 −8.142 −2.430 −21.890 1.00 1.00 H ATOM 2521 N CYS A 1136 −6.703 −1.384 −19.118 1.00 1.00 N ATOM 2522 CA CYS A 1136 −6.169 −1.260 −17.793 1.00 1.00 C ATOM 2523 C CYS A 1136 −5.008 −2.168 −17.671 1.00 1.00 C ATOM 2524 O CYS A 1136 −3.912 −1.759 −17.253 1.00 1.00 O ATOM 2525 CB CYS A 1136 −7.148 −1.561 −16.614 1.00 1.00 C ATOM 2526 SG CYS A 1136 −8.668 −0.524 −16.550 1.00 1.00 S ATOM 2527 HA CYS A 1136 −5.856 −0.226 −17.702 1.00 1.00 H ATOM 2528 HB1 CYS A 1136 −7.444 −2.627 −16.544 1.00 1.00 H ATOM 2529 HB2 CYS A 1136 −6.658 −1.359 −15.625 1.00 1.00 H ATOM 2530 HG CYS A 1136 −8.854 −0.518 −15.536 1.00 1.00 H ATOM 2531 HN CYS A 1136 −7.613 −1.714 −19.285 1.00 1.00 H ATOM 2532 N SER A 1137 −5.153 −3.427 −18.041 1.00 1.00 N ATOM 2533 CA SER A 1137 −3.988 −4.337 −18.028 1.00 1.00 C ATOM 2534 C SER A 1137 −2.743 −3.650 −18.636 1.00 1.00 C ATOM 2535 O SER A 1137 −1.763 −3.564 −17.943 1.00 1.00 O ATOM 2536 CB SER A 1137 −4.329 −5.748 −18.488 1.00 1.00 C ATOM 2537 OG SER A 1137 −3.130 −6.487 −18.749 1.00 1.00 O ATOM 2538 HA SER A 1137 −3.687 −4.375 −16.989 1.00 1.00 H ATOM 2539 HB1 SER A 1137 −4.909 −5.517 −19.422 1.00 1.00 H ATOM 2540 HB2 SER A 1137 −5.039 −6.248 −17.822 1.00 1.00 H ATOM 2541 HG SER A 1137 −2.760 −6.824 −17.966 1.00 1.00 H ATOM 2542 HN SER A 1137 −6.113 −3.723 −18.329 1.00 1.00 H ATOM 2543 N ARG A 1138 −2.760 −3.135 −19.883 1.00 1.00 N ATOM 2544 CA ARG A 1138 −1.490 −2.506 −20.364 1.00 1.00 C ATOM 2545 C ARG A 1138 −1.156 −1.347 −19.425 1.00 1.00 C ATOM 2546 O ARG A 1138 −0.035 −1.273 −18.948 1.00 1.00 O ATOM 2547 CB ARG A 1138 −1.474 −1.985 −21.854 1.00 1.00 C ATOM 2548 CG ARG A 1138 −0.850 −2.958 −22.900 1.00 1.00 C ATOM 2549 CD ARG A 1138 −1.951 −4.003 −23.330 1.00 1.00 C ATOM 2550 NE ARG A 1138 −2.270 −5.014 −22.332 1.00 1.00 N ATOM 2551 CZ ARG A 1138 −3.078 −6.021 −22.571 1.00 1.00 C ATOM 2552 NH1 ARG A 1138 −3.594 −6.290 −23.761 1.00 1.00 N ATOM 2553 NH2 ARG A 1138 −3.413 −6.877 −21.631 1.00 1.00 N ATOM 2554 HA ARG A 1138 −0.662 −3.208 −20.295 1.00 1.00 H ATOM 2555 HB1 ARG A 1138 −0.851 −1.067 −21.890 1.00 1.00 H ATOM 2556 HB2 ARG A 1138 −2.433 −1.533 −22.129 1.00 1.00 H ATOM 2557 HG1 ARG A 1138 0.097 −3.431 −22.566 1.00 1.00 H ATOM 2558 HG2 ARG A 1138 −0.597 −2.335 −23.760 1.00 1.00 H ATOM 2559 HD1 ARG A 1138 −1.663 −4.571 −24.152 1.00 1.00 H ATOM 2560 HD2 ARG A 1138 −2.886 −3.446 −23.541 1.00 1.00 H ATOM 2561 HE ARG A 1138 −1.822 −5.016 −21.444 1.00 1.00 H ATOM 2562 HH12 ARG A 1138 −4.216 −7.071 −23.937 1.00 1.00 H ATOM 2563 HH11 ARG A 1138 −3.449 −5.624 −24.533 1.00 1.00 H ATOM 2564 HH22 ARG A 1138 −4.175 −7.548 −21.819 1.00 1.00 H ATOM 2565 HH21 ARG A 1138 −2.961 −6.846 −20.686 1.00 1.00 H ATOM 2566 HN ARG A 1138 −3.593 −3.108 −20.451 1.00 1.00 H ATOM 2567 N ASN A 1139 −2.124 −0.442 −19.278 1.00 1.00 N ATOM 2568 CA ASN A 1139 −1.752 0.806 −18.613 1.00 1.00 C ATOM 2569 C ASN A 1139 −1.276 0.533 −17.233 1.00 1.00 C ATOM 2570 O ASN A 1139 −0.390 1.278 −16.803 1.00 1.00 O ATOM 2571 CB ASN A 1139 −2.940 1.775 −18.582 1.00 1.00 C ATOM 2572 CG ASN A 1139 −2.470 3.027 −17.912 1.00 1.00 C ATOM 2573 OD1 ASN A 1139 −1.704 3.783 −18.533 1.00 1.00 O ATOM 2574 ND2 ASN A 1139 −2.887 3.279 −16.637 1.00 1.00 N ATOM 2575 HA ASN A 1139 −0.924 1.282 −19.175 1.00 1.00 H ATOM 2576 HB1 ASN A 1139 −3.830 1.377 −18.085 1.00 1.00 H ATOM 2577 HB2 ASN A 1139 −3.232 1.964 −19.623 1.00 1.00 H ATOM 2578 HD22 ASN A 1139 −2.557 4.103 −16.179 1.00 1.00 H ATOM 2579 HD21 ASN A 1139 −3.442 2.708 −16.055 1.00 1.00 H ATOM 2580 HN ASN A 1139 −3.046 −0.681 −19.541 1.00 1.00 H ATOM 2581 N LEU A 1140 −1.825 −0.469 −16.511 1.00 1.00 N ATOM 2582 CA LEU A 1140 −1.503 −0.630 −15.134 1.00 1.00 C ATOM 2583 C LEU A 1140 −0.074 −1.001 −15.080 1.00 1.00 C ATOM 2584 O LEU A 1140 0.668 −0.256 −14.438 1.00 1.00 O ATOM 2585 CB LEU A 1140 −2.462 −1.726 −14.560 1.00 1.00 C ATOM 2586 CG LEU A 1140 −2.349 −1.891 −12.978 1.00 1.00 C ATOM 2587 CD1 LEU A 1140 −3.437 −2.862 −12.414 1.00 1.00 C ATOM 2588 CD2 LEU A 1140 −0.947 −2.342 −12.573 1.00 1.00 C ATOM 2589 HA LEU A 1140 −1.676 0.283 −14.549 1.00 1.00 H ATOM 2590 HB1 LEU A 1140 −2.280 −2.719 −15.105 1.00 1.00 H ATOM 2591 HB2 LEU A 1140 −3.494 −1.358 −14.755 1.00 1.00 H ATOM 2592 HG LEU A 1140 −2.530 −0.880 −12.549 1.00 1.00 H ATOM 2593 HD21 LEU A 1140 −0.988 −2.519 −11.465 1.00 1.00 H ATOM 2594 HD22 LEU A 1140 −0.258 −1.577 −12.562 1.00 1.00 H ATOM 2595 HD23 LEU A 1140 −0.619 −3.217 −13.135 1.00 1.00 H ATOM 2596 HD11 LEU A 1140 −3.229 −3.916 −12.710 1.00 1.00 H ATOM 2597 HD12 LEU A 1140 −4.398 −2.528 −12.848 1.00 1.00 H ATOM 2598 HD13 LEU A 1140 −3.490 −2.815 −11.339 1.00 1.00 H ATOM 2599 HN LEU A 1140 −2.322 −1.190 −16.955 1.00 1.00 H ATOM 2600 N TYR A 1141 0.383 −2.084 −15.689 1.00 1.00 N ATOM 2601 CA TYR A 1141 1.784 −2.353 −15.613 1.00 1.00 C ATOM 2602 C TYR A 1141 2.679 −1.397 −16.383 1.00 1.00 C ATOM 2603 O TYR A 1141 3.718 −0.994 −15.902 1.00 1.00 O ATOM 2604 CB TYR A 1141 2.156 −3.870 −15.820 1.00 1.00 C ATOM 2605 CG TYR A 1141 1.799 −4.310 −17.206 1.00 1.00 C ATOM 2606 CD1 TYR A 1141 0.658 −5.128 −17.411 1.00 1.00 C ATOM 2607 CD2 TYR A 1141 2.555 −3.963 −18.324 1.00 1.00 C ATOM 2608 CE1 TYR A 1141 0.424 −5.669 −18.677 1.00 1.00 C ATOM 2609 CE2 TYR A 1141 2.283 −4.471 −19.595 1.00 1.00 C ATOM 2610 CZ TYR A 1141 1.179 −5.303 −19.809 1.00 1.00 C ATOM 2611 OH TYR A 1141 0.806 −5.678 −21.128 1.00 1.00 O ATOM 2612 HA TYR A 1141 2.132 −2.211 −14.595 1.00 1.00 H ATOM 2613 HB2 TYR A 1141 1.532 −4.530 −15.146 1.00 1.00 H ATOM 2614 HB1 TYR A 1141 3.187 −4.133 −15.579 1.00 1.00 H ATOM 2615 HD2 TYR A 1141 3.406 −3.278 −18.207 1.00 1.00 H ATOM 2616 HE2 TYR A 1141 2.965 −4.271 −20.413 1.00 1.00 H ATOM 2617 HE1 TYR A 1141 −0.403 −6.375 −18.788 1.00 1.00 H ATOM 2618 HD1 TYR A 1141 −0.041 −5.288 −16.591 1.00 1.00 H ATOM 2619 HH TYR A 1141 0.986 −6.622 −21.139 1.00 1.00 H ATOM 2620 HN TYR A 1141 −0.164 −2.669 −16.233 1.00 1.00 H ATOM 2621 N VAL A 1142 2.284 −0.965 −17.573 1.00 1.00 N ATOM 2622 CA VAL A 1142 3.132 0.003 −18.277 1.00 1.00 C ATOM 2623 C VAL A 1142 3.272 1.322 −17.482 1.00 1.00 C ATOM 2624 O VAL A 1142 4.414 1.753 −17.297 1.00 1.00 O ATOM 2625 CB VAL A 1142 2.604 0.393 −19.704 1.00 1.00 C ATOM 2626 CG1 VAL A 1142 3.428 1.535 −20.262 1.00 1.00 C ATOM 2627 CG2 VAL A 1142 2.523 −0.771 −20.695 1.00 1.00 C ATOM 2628 HA VAL A 1142 4.140 −0.442 −18.370 1.00 1.00 H ATOM 2629 HB VAL A 1142 1.562 0.790 −19.559 1.00 1.00 H ATOM 2630 HG11 VAL A 1142 4.498 1.335 −20.198 1.00 1.00 H ATOM 2631 HG12 VAL A 1142 3.225 2.481 −19.773 1.00 1.00 H ATOM 2632 HG13 VAL A 1142 3.118 1.704 −21.325 1.00 1.00 H ATOM 2633 HG21 VAL A 1142 3.502 −0.993 −21.152 1.00 1.00 H ATOM 2634 HG22 VAL A 1142 1.806 −0.510 −21.502 1.00 1.00 H ATOM 2635 HG23 VAL A 1142 2.227 −1.734 −20.170 1.00 1.00 H ATOM 2636 HN VAL A 1142 1.421 −1.248 −17.995 1.00 1.00 H ATOM 2637 N SER A 1143 2.189 1.974 −17.006 1.00 1.00 N ATOM 2638 CA SER A 1143 2.399 3.147 −16.103 1.00 1.00 C ATOM 2639 C SER A 1143 3.138 2.754 −14.853 1.00 1.00 C ATOM 2640 O SER A 1143 4.127 3.430 −14.600 1.00 1.00 O ATOM 2641 CB SER A 1143 1.022 3.809 −15.734 1.00 1.00 C ATOM 2642 OG SER A 1143 0.162 2.970 −14.923 1.00 1.00 O ATOM 2643 HA SER A 1143 3.028 3.886 −16.594 1.00 1.00 H ATOM 2644 HB1 SER A 1143 0.470 4.114 −16.650 1.00 1.00 H ATOM 2645 HB2 SER A 1143 1.135 4.652 −15.026 1.00 1.00 H ATOM 2646 HG SER A 1143 −0.274 2.263 −15.371 1.00 1.00 H ATOM 2647 HN SER A 1143 1.322 1.603 −17.291 1.00 1.00 H ATOM 2648 N LEU A 1144 2.700 1.761 −14.113 1.00 1.00 N ATOM 2649 CA LEU A 1144 3.449 1.426 −12.920 1.00 1.00 C ATOM 2650 C LEU A 1144 4.926 1.275 −13.269 1.00 1.00 C ATOM 2651 O LEU A 1144 5.698 1.915 −12.547 1.00 1.00 O ATOM 2652 CB LEU A 1144 2.918 0.101 −12.260 1.00 1.00 C ATOM 2653 CG LEU A 1144 3.749 −0.319 −11.032 1.00 1.00 C ATOM 2654 CD1 LEU A 1144 3.862 0.771 −9.974 1.00 1.00 C ATOM 2655 CD2 LEU A 1144 3.087 −1.598 −10.405 1.00 1.00 C ATOM 2656 HA LEU A 1144 3.253 2.264 −12.202 1.00 1.00 H ATOM 2657 HB1 LEU A 1144 2.919 −0.739 −12.963 1.00 1.00 H ATOM 2658 HB2 LEU A 1144 1.863 0.233 −11.967 1.00 1.00 H ATOM 2659 HG LEU A 1144 4.791 −0.474 −11.397 1.00 1.00 H ATOM 2660 HD21 LEU A 1144 2.063 −1.472 −9.994 1.00 1.00 H ATOM 2661 HD22 LEU A 1144 3.780 −1.890 −9.612 1.00 1.00 H ATOM 2662 HD23 LEU A 1144 3.016 −2.422 −11.174 1.00 1.00 H ATOM 2663 HD11 LEU A 1144 4.432 0.414 −9.119 1.00 1.00 H ATOM 2664 HD12 LEU A 1144 2.892 1.166 −9.734 1.00 1.00 H ATOM 2665 HD13 LEU A 1144 4.468 1.609 −10.331 1.00 1.00 H ATOM 2666 HN LEU A 1144 1.830 1.316 −14.291 1.00 1.00 H ATOM 2667 N LEU A 1145 5.369 0.609 −14.367 1.00 1.00 N ATOM 2668 CA LEU A 1145 6.798 0.419 −14.652 1.00 1.00 C ATOM 2669 C LEU A 1145 7.504 1.774 −14.700 1.00 1.00 C ATOM 2670 O LEU A 1145 8.503 2.007 −14.047 1.00 1.00 O ATOM 2671 CB LEU A 1145 6.962 −0.392 −15.994 1.00 1.00 C ATOM 2672 CG LEU A 1145 8.499 −0.559 −16.314 1.00 1.00 C ATOM 2673 CD1 LEU A 1145 9.206 −1.431 −15.196 1.00 1.00 C ATOM 2674 CD2 LEU A 1145 8.648 −1.290 −17.707 1.00 1.00 C ATOM 2675 HA LEU A 1145 7.210 −0.120 −13.827 1.00 1.00 H ATOM 2676 HB1 LEU A 1145 6.511 0.200 −16.814 1.00 1.00 H ATOM 2677 HB2 LEU A 1145 6.423 −1.338 −15.793 1.00 1.00 H ATOM 2678 HG LEU A 1145 9.128 0.379 −16.455 1.00 1.00 H ATOM 2679 HD21 LEU A 1145 9.725 −1.542 −17.850 1.00 1.00 H ATOM 2680 HD22 LEU A 1145 8.432 −0.590 −18.517 1.00 1.00 H ATOM 2681 HD23 LEU A 1145 8.079 −2.249 −17.837 1.00 1.00 H ATOM 2682 HD11 LEU A 1145 10.154 −1.845 −15.455 1.00 1.00 H ATOM 2683 HD12 LEU A 1145 8.562 −2.304 −15.116 1.00 1.00 H ATOM 2684 HD13 LEU A 1145 9.309 −1.009 −14.204 1.00 1.00 H ATOM 2685 HN LEU A 1145 4.696 0.273 −15.011 1.00 1.00 H ATOM 2686 N LEU A 1146 6.918 2.685 −15.464 1.00 1.00 N ATOM 2687 CA LEU A 1146 7.442 4.036 −15.545 1.00 1.00 C ATOM 2688 C LEU A 1146 7.495 4.730 −14.233 1.00 1.00 C ATOM 2689 O LEU A 1146 8.443 5.460 −13.920 1.00 1.00 O ATOM 2690 CB LEU A 1146 6.649 4.932 −16.550 1.00 1.00 C ATOM 2691 CG LEU A 1146 6.662 4.517 −18.052 1.00 1.00 C ATOM 2692 CD1 LEU A 1146 5.685 5.455 −18.843 1.00 1.00 C ATOM 2693 CD2 LEU A 1146 8.091 4.619 −18.721 1.00 1.00 C ATOM 2694 HA LEU A 1146 8.434 3.905 −15.894 1.00 1.00 H ATOM 2695 HB1 LEU A 1146 7.122 5.948 −16.481 1.00 1.00 H ATOM 2696 HB2 LEU A 1146 5.597 4.987 −16.189 1.00 1.00 H ATOM 2697 HG LEU A 1146 6.378 3.480 −18.230 1.00 1.00 H ATOM 2698 HD21 LEU A 1146 8.037 4.511 −19.805 1.00 1.00 H ATOM 2699 HD22 LEU A 1146 8.773 3.757 −18.392 1.00 1.00 H ATOM 2700 HD23 LEU A 1146 8.543 5.582 −18.532 1.00 1.00 H ATOM 2701 HD11 LEU A 1146 4.643 5.534 −18.439 1.00 1.00 H ATOM 2702 HD12 LEU A 1146 5.577 5.272 −19.932 1.00 1.00 H ATOM 2703 HD13 LEU A 1146 6.093 6.510 −18.691 1.00 1.00 H ATOM 2704 HN LEU A 1146 6.093 2.485 −15.953 1.00 1.00 H ATOM 2705 N LEU A 1147 6.472 4.539 −13.418 1.00 1.00 N ATOM 2706 CA LEU A 1147 6.426 5.262 −12.130 1.00 1.00 C ATOM 2707 C LEU A 1147 7.496 4.727 −11.210 1.00 1.00 C ATOM 2708 O LEU A 1147 8.312 5.455 −10.630 1.00 1.00 O ATOM 2709 CB LEU A 1147 5.079 5.276 −11.412 1.00 1.00 C ATOM 2710 CG LEU A 1147 3.905 5.942 −12.191 1.00 1.00 C ATOM 2711 CD1 LEU A 1147 2.548 5.729 −11.449 1.00 1.00 C ATOM 2712 CD2 LEU A 1147 4.228 7.452 −12.438 1.00 1.00 C ATOM 2713 HA LEU A 1147 6.744 6.293 −12.341 1.00 1.00 H ATOM 2714 HB1 LEU A 1147 5.234 5.778 −10.454 1.00 1.00 H ATOM 2715 HB2 LEU A 1147 4.738 4.274 −11.155 1.00 1.00 H ATOM 2716 HG LEU A 1147 3.716 5.481 −13.166 1.00 1.00 H ATOM 2717 HD21 LEU A 1147 5.122 7.611 −13.082 1.00 1.00 H ATOM 2718 HD22 LEU A 1147 4.357 7.997 −11.499 1.00 1.00 H ATOM 2719 HD23 LEU A 1147 3.431 7.933 −12.956 1.00 1.00 H ATOM 2720 HD11 LEU A 1147 2.317 4.705 −11.189 1.00 1.00 H ATOM 2721 HD12 LEU A 1147 1.694 6.176 −12.045 1.00 1.00 H ATOM 2722 HD13 LEU A 1147 2.488 6.344 −10.524 1.00 1.00 H ATOM 2723 HN LEU A 1147 5.773 3.835 −13.611 1.00 1.00 H ATOM 2724 N TYR A 1148 7.635 3.388 −11.003 1.00 1.00 N ATOM 2725 CA TYR A 1148 8.811 2.908 −10.275 1.00 1.00 C ATOM 2726 C TYR A 1148 10.073 3.391 −10.974 1.00 1.00 C ATOM 2727 O TYR A 1148 10.958 3.922 −10.372 1.00 1.00 O ATOM 2728 CB TYR A 1148 8.908 1.365 −10.235 1.00 1.00 C ATOM 2729 CG TYR A 1148 10.112 0.898 −9.422 1.00 1.00 C ATOM 2730 CD1 TYR A 1148 11.403 0.925 −9.966 1.00 1.00 C ATOM 2731 CD2 TYR A 1148 9.959 0.446 −8.092 1.00 1.00 C ATOM 2732 CE1 TYR A 1148 12.535 0.612 −9.198 1.00 1.00 C ATOM 2733 CE2 TYR A 1148 11.075 0.090 −7.346 1.00 1.00 C ATOM 2734 CZ TYR A 1148 12.367 0.063 −7.914 1.00 1.00 C ATOM 2735 OH TYR A 1148 13.452 −0.458 −7.222 1.00 1.00 O ATOM 2736 HA TYR A 1148 8.771 3.256 −9.232 1.00 1.00 H ATOM 2737 HB2 TYR A 1148 8.886 0.836 −11.209 1.00 1.00 H ATOM 2738 HB1 TYR A 1148 7.989 1.022 −9.710 1.00 1.00 H ATOM 2739 HD2 TYR A 1148 8.971 0.366 −7.706 1.00 1.00 H ATOM 2740 HE2 TYR A 1148 10.967 −0.221 −6.282 1.00 1.00 H ATOM 2741 HE1 TYR A 1148 13.517 0.683 −9.556 1.00 1.00 H ATOM 2742 HD1 TYR A 1148 11.486 1.142 −11.005 1.00 1.00 H ATOM 2743 HH TYR A 1148 13.851 −1.056 −7.845 1.00 1.00 H ATOM 2744 HN TYR A 1148 7.046 2.706 −11.417 1.00 1.00 H ATOM 2745 N GLN A 1149 10.219 3.224 −12.304 1.00 1.00 N ATOM 2746 CA GLN A 1149 11.443 3.687 −12.927 1.00 1.00 C ATOM 2747 C GLN A 1149 11.689 5.187 −12.632 1.00 1.00 C ATOM 2748 O GLN A 1149 12.853 5.538 −12.515 1.00 1.00 O ATOM 2749 CB GLN A 1149 11.256 3.587 −14.433 1.00 1.00 C ATOM 2750 CG GLN A 1149 12.600 3.911 −15.217 1.00 1.00 C ATOM 2751 CD GLN A 1149 12.503 3.860 −16.762 1.00 1.00 C ATOM 2752 OE1 GLN A 1149 13.057 2.975 −17.381 1.00 1.00 O ATOM 2753 NE2 GLN A 1149 11.849 4.793 −17.445 1.00 1.00 N ATOM 2754 HA GLN A 1149 12.323 3.126 −12.571 1.00 1.00 H ATOM 2755 HB1 GLN A 1149 10.522 4.339 −14.776 1.00 1.00 H ATOM 2756 HB2 GLN A 1149 10.988 2.572 −14.723 1.00 1.00 H ATOM 2757 HG1 GLN A 1149 13.459 3.304 −14.947 1.00 1.00 H ATOM 2758 HG2 GLN A 1149 12.926 4.936 −14.961 1.00 1.00 H ATOM 2759 HE22 GLN A 1149 11.874 4.753 −18.448 1.00 1.00 H ATOM 2760 HE21 GLN A 1149 11.329 5.515 −16.973 1.00 1.00 H ATOM 2761 HN GLN A 1149 9.475 2.777 −12.848 1.00 1.00 H ATOM 2762 N THR A 1150 10.591 6.021 −12.564 1.00 1.00 N ATOM 2763 CA THR A 1150 10.744 7.475 −12.380 1.00 1.00 C ATOM 2764 C THR A 1150 11.060 7.796 −10.909 1.00 1.00 C ATOM 2765 O THR A 1150 12.048 8.480 −10.651 1.00 1.00 O ATOM 2766 CB THR A 1150 9.564 8.339 −12.824 1.00 1.00 C ATOM 2767 OG1 THR A 1150 9.436 8.261 −14.284 1.00 1.00 O ATOM 2768 CG2 THR A 1150 9.873 9.776 −12.396 1.00 1.00 C ATOM 2769 HA THR A 1150 11.636 7.836 −12.963 1.00 1.00 H ATOM 2770 HB THR A 1150 8.563 8.084 −12.381 1.00 1.00 H ATOM 2771 HG1 THR A 1150 9.073 7.425 −14.633 1.00 1.00 H ATOM 2772 HG23 THR A 1150 9.207 10.489 −12.807 1.00 1.00 H ATOM 2773 HG21 THR A 1150 10.835 10.125 −12.854 1.00 1.00 H ATOM 2774 HG22 THR A 1150 9.912 9.914 −11.331 1.00 1.00 H ATOM 2775 HN THR A 1150 9.627 5.761 −12.622 1.00 1.00 H ATOM 2776 N PHE A 1151 10.294 7.233 −9.883 1.00 1.00 N ATOM 2777 CA PHE A 1151 10.556 7.501 −8.450 1.00 1.00 C ATOM 2778 C PHE A 1151 11.306 6.307 −7.827 1.00 1.00 C ATOM 2779 O PHE A 1151 12.359 6.487 −7.220 1.00 1.00 O ATOM 2780 CB PHE A 1151 9.212 7.887 −7.671 1.00 1.00 C ATOM 2781 CG PHE A 1151 8.631 8.999 −8.531 1.00 1.00 C ATOM 2782 CD1 PHE A 1151 9.287 10.240 −8.573 1.00 1.00 C ATOM 2783 CD2 PHE A 1151 7.530 8.747 −9.346 1.00 1.00 C ATOM 2784 CE1 PHE A 1151 8.839 11.187 −9.500 1.00 1.00 C ATOM 2785 CE2 PHE A 1151 7.169 9.679 −10.309 1.00 1.00 C ATOM 2786 CZ PHE A 1151 7.801 10.902 −10.380 1.00 1.00 C ATOM 2787 HA PHE A 1151 11.298 8.301 −8.417 1.00 1.00 H ATOM 2788 HB1 PHE A 1151 9.356 8.287 −6.641 1.00 1.00 H ATOM 2789 HB2 PHE A 1151 8.535 7.032 −7.662 1.00 1.00 H ATOM 2790 HD2 PHE A 1151 6.971 7.846 −9.252 1.00 1.00 H ATOM 2791 HE2 PHE A 1151 6.335 9.380 −10.999 1.00 1.00 H ATOM 2792 HZ PHE A 1151 7.549 11.606 −11.159 1.00 1.00 H ATOM 2793 HE1 PHE A 1151 9.359 12.146 −9.558 1.00 1.00 H ATOM 2794 HD1 PHE A 1151 10.026 10.410 −7.850 1.00 1.00 H ATOM 2795 HN PHE A 1151 9.534 6.684 −10.145 1.00 1.00 H ATOM 2796 N GLY A 1152 10.678 5.116 −7.944 1.00 1.00 N ATOM 2797 CA GLY A 1152 11.260 3.951 −7.322 1.00 1.00 C ATOM 2798 C GLY A 1152 11.359 3.942 −5.869 1.00 1.00 C ATOM 2799 O GLY A 1152 10.586 3.257 −5.193 1.00 1.00 O ATOM 2800 HA2 GLY A 1152 12.251 3.836 −7.787 1.00 1.00 H ATOM 2801 HA1 GLY A 1152 10.669 3.030 −7.635 1.00 1.00 H ATOM 2802 HN GLY A 1152 9.824 5.093 −8.451 1.00 1.00 H ATOM 2803 N ARG A 1153 12.328 4.704 −5.332 1.00 1.00 N ATOM 2804 CA ARG A 1153 12.698 4.574 −3.931 1.00 1.00 C ATOM 2805 C ARG A 1153 12.956 5.904 −3.260 1.00 1.00 C ATOM 2806 O ARG A 1153 13.006 6.858 −4.013 1.00 1.00 O ATOM 2807 CB ARG A 1153 13.924 3.600 −3.885 1.00 1.00 C ATOM 2808 CG ARG A 1153 13.435 2.139 −4.075 1.00 1.00 C ATOM 2809 CD ARG A 1153 14.566 1.045 −4.103 1.00 1.00 C ATOM 2810 NE ARG A 1153 13.920 −0.191 −4.490 1.00 1.00 N ATOM 2811 CZ ARG A 1153 13.389 −0.997 −3.593 1.00 1.00 C ATOM 2812 NH1 ARG A 1153 13.407 −0.844 −2.298 1.00 1.00 N ATOM 2813 NH2 ARG A 1153 12.720 −1.994 −4.101 1.00 1.00 N ATOM 2814 HA ARG A 1153 11.814 4.217 −3.359 1.00 1.00 H ATOM 2815 HB1 ARG A 1153 14.448 3.728 −2.939 1.00 1.00 H ATOM 2816 HB2 ARG A 1153 14.676 3.819 −4.699 1.00 1.00 H ATOM 2817 HG1 ARG A 1153 12.951 2.076 −5.021 1.00 1.00 H ATOM 2818 HG2 ARG A 1153 12.701 1.812 −3.267 1.00 1.00 H ATOM 2819 HD1 ARG A 1153 15.202 1.099 −3.260 1.00 1.00 H ATOM 2820 HD2 ARG A 1153 15.264 1.417 −4.894 1.00 1.00 H ATOM 2821 HE ARG A 1153 13.874 −0.374 −5.512 1.00 1.00 H ATOM 2822 HH12 ARG A 1153 12.833 −1.483 −1.758 1.00 1.00 H ATOM 2823 HH11 ARG A 1153 14.027 −0.175 −1.807 1.00 1.00 H ATOM 2824 HH22 ARG A 1153 12.271 −2.669 −3.458 1.00 1.00 H ATOM 2825 HH21 ARG A 1153 12.614 −2.141 −5.096 1.00 1.00 H ATOM 2826 HN ARG A 1153 12.963 5.221 −5.880 1.00 1.00 H ATOM 2827 N LYS A 1154 13.123 6.053 −1.922 1.00 1.00 N ATOM 2828 CA LYS A 1154 12.885 5.004 −0.957 1.00 1.00 C ATOM 2829 C LYS A 1154 11.483 5.298 −0.382 1.00 1.00 C ATOM 2830 O LYS A 1154 11.440 6.156 0.480 1.00 1.00 O ATOM 2831 CB LYS A 1154 14.028 5.115 0.083 1.00 1.00 C ATOM 2832 CG LYS A 1154 13.714 4.114 1.242 1.00 1.00 C ATOM 2833 CD LYS A 1154 14.699 4.185 2.419 1.00 1.00 C ATOM 2834 CE LYS A 1154 14.550 3.088 3.518 1.00 1.00 C ATOM 2835 NZ LYS A 1154 14.928 1.682 3.208 1.00 1.00 N ATOM 2836 HA LYS A 1154 12.847 3.988 −1.343 1.00 1.00 H ATOM 2837 HB1 LYS A 1154 14.060 6.127 0.459 1.00 1.00 H ATOM 2838 HB2 LYS A 1154 14.956 4.857 −0.417 1.00 1.00 H ATOM 2839 HG1 LYS A 1154 13.754 3.086 0.819 1.00 1.00 H ATOM 2840 HG2 LYS A 1154 12.772 4.250 1.740 1.00 1.00 H ATOM 2841 HD1 LYS A 1154 14.559 5.190 2.845 1.00 1.00 H ATOM 2842 HD2 LYS A 1154 15.753 4.078 2.079 1.00 1.00 H ATOM 2843 HE1 LYS A 1154 13.478 3.095 3.743 1.00 1.00 H ATOM 2844 HE2 LYS A 1154 15.038 3.438 4.413 1.00 1.00 H ATOM 2845 HZ1 LYS A 1154 14.808 1.217 4.145 1.00 1.00 H ATOM 2846 HZ2 LYS A 1154 15.916 1.486 2.925 1.00 1.00 H ATOM 2847 HZ3 LYS A 1154 14.326 1.121 2.448 1.00 1.00 H ATOM 2848 HN LYS A 1154 13.261 6.982 −1.580 1.00 1.00 H ATOM 2849 N LEU A 1155 10.368 4.584 −0.750 1.00 1.00 N ATOM 2850 CA LEU A 1155 9.192 4.686 0.056 1.00 1.00 C ATOM 2851 C LEU A 1155 9.454 4.272 1.528 1.00 1.00 C ATOM 2852 O LEU A 1155 9.425 3.096 1.843 1.00 1.00 O ATOM 2853 CB LEU A 1155 8.070 3.732 −0.516 1.00 1.00 C ATOM 2854 CG LEU A 1155 6.733 3.804 0.233 1.00 1.00 C ATOM 2855 CD1 LEU A 1155 6.017 5.197 0.245 1.00 1.00 C ATOM 2856 CD2 LEU A 1155 5.779 2.774 −0.382 1.00 1.00 C ATOM 2857 HA LEU A 1155 8.899 5.768 0.040 1.00 1.00 H ATOM 2858 HB1 LEU A 1155 8.525 2.739 −0.516 1.00 1.00 H ATOM 2859 HB2 LEU A 1155 7.831 4.106 −1.548 1.00 1.00 H ATOM 2860 HG LEU A 1155 6.798 3.641 1.377 1.00 1.00 H ATOM 2861 HD21 LEU A 1155 6.137 1.752 −0.319 1.00 1.00 H ATOM 2862 HD22 LEU A 1155 5.518 3.025 −1.400 1.00 1.00 H ATOM 2863 HD23 LEU A 1155 4.827 2.798 0.218 1.00 1.00 H ATOM 2864 HD11 LEU A 1155 5.743 5.472 −0.762 1.00 1.00 H ATOM 2865 HD12 LEU A 1155 6.682 5.959 0.634 1.00 1.00 H ATOM 2866 HD13 LEU A 1155 5.069 5.216 0.849 1.00 1.00 H ATOM 2867 HN LEU A 1155 10.423 3.905 −1.482 1.00 1.00 H ATOM 2868 N HIS A 1156 9.737 5.208 2.450 1.00 1.00 N ATOM 2869 CA HIS A 1156 9.937 4.900 3.870 1.00 1.00 C ATOM 2870 C HIS A 1156 8.638 4.596 4.513 1.00 1.00 C ATOM 2871 O HIS A 1156 8.137 5.370 5.304 1.00 1.00 O ATOM 2872 CB HIS A 1156 10.778 6.053 4.518 1.00 1.00 C ATOM 2873 CG HIS A 1156 11.137 5.771 5.990 1.00 1.00 C ATOM 2874 ND1 HIS A 1156 10.280 5.762 7.009 1.00 1.00 N ATOM 2875 CD2 HIS A 1156 12.395 5.511 6.428 1.00 1.00 C ATOM 2876 CE1 HIS A 1156 10.983 5.441 8.080 1.00 1.00 C ATOM 2877 NE2 HIS A 1156 12.187 5.303 7.828 1.00 1.00 N ATOM 2878 HA HIS A 1156 10.555 3.969 3.846 1.00 1.00 H ATOM 2879 HB1 HIS A 1156 10.215 6.990 4.425 1.00 1.00 H ATOM 2880 HB2 HIS A 1156 11.651 6.133 3.910 1.00 1.00 H ATOM 2881 HD2 HIS A 1156 13.319 5.448 5.878 1.00 1.00 H ATOM 2882 HE1 HIS A 1156 10.519 5.296 9.076 1.00 1.00 H ATOM 2883 HD1 HIS A 1156 9.234 5.916 6.960 1.00 1.00 H ATOM 2884 HN HIS A 1156 9.803 6.186 2.155 1.00 1.00 H ATOM 2885 N LEU A 1157 8.056 3.445 4.117 1.00 1.00 N ATOM 2886 CA LEU A 1157 6.794 2.916 4.719 1.00 1.00 C ATOM 2887 C LEU A 1157 7.007 2.809 6.217 1.00 1.00 C ATOM 2888 O LEU A 1157 8.154 2.531 6.571 1.00 1.00 O ATOM 2889 CB LEU A 1157 6.297 1.635 3.970 1.00 1.00 C ATOM 2890 CG LEU A 1157 5.014 0.959 4.584 1.00 1.00 C ATOM 2891 CD1 LEU A 1157 4.339 0.197 3.476 1.00 1.00 C ATOM 2892 CD2 LEU A 1157 5.392 −0.021 5.734 1.00 1.00 C ATOM 2893 HA LEU A 1157 6.037 3.672 4.525 1.00 1.00 H ATOM 2894 HB1 LEU A 1157 7.114 0.885 4.019 1.00 1.00 H ATOM 2895 HB2 LEU A 1157 6.159 1.863 2.912 1.00 1.00 H ATOM 2896 HG LEU A 1157 4.421 1.723 5.056 1.00 1.00 H ATOM 2897 HD21 LEU A 1157 4.528 −0.445 6.240 1.00 1.00 H ATOM 2898 HD22 LEU A 1157 6.064 0.440 6.497 1.00 1.00 H ATOM 2899 HD23 LEU A 1157 6.005 −0.778 5.302 1.00 1.00 H ATOM 2900 HD11 LEU A 1157 5.089 −0.382 2.889 1.00 1.00 H ATOM 2901 HD12 LEU A 1157 3.688 −0.601 3.806 1.00 1.00 H ATOM 2902 HD13 LEU A 1157 3.823 0.950 2.853 1.00 1.00 H ATOM 2903 HN LEU A 1157 8.415 2.896 3.377 1.00 1.00 H ATOM 2904 N TYR A 1158 6.001 2.997 7.112 1.00 1.00 N ATOM 2905 CA TYR A 1158 6.353 2.691 8.492 1.00 1.00 C ATOM 2906 C TYR A 1158 5.180 2.340 9.420 1.00 1.00 C ATOM 2907 O TYR A 1158 5.231 2.582 10.620 1.00 1.00 O ATOM 2908 CB TYR A 1158 7.108 3.911 9.064 1.00 1.00 C ATOM 2909 CG TYR A 1158 6.248 5.186 9.219 1.00 1.00 C ATOM 2910 CD1 TYR A 1158 5.856 5.665 10.473 1.00 1.00 C ATOM 2911 CD2 TYR A 1158 5.938 5.989 8.107 1.00 1.00 C ATOM 2912 CE1 TYR A 1158 5.305 6.954 10.640 1.00 1.00 C ATOM 2913 CE2 TYR A 1158 5.365 7.274 8.256 1.00 1.00 C ATOM 2914 CZ TYR A 1158 5.140 7.799 9.536 1.00 1.00 C ATOM 2915 OH TYR A 1158 4.730 9.142 9.708 1.00 1.00 O ATOM 2916 HA TYR A 1158 6.993 1.801 8.552 1.00 1.00 H ATOM 2917 HB2 TYR A 1158 7.952 4.117 8.428 1.00 1.00 H ATOM 2918 HB1 TYR A 1158 7.505 3.602 10.063 1.00 1.00 H ATOM 2919 HD2 TYR A 1158 6.128 5.658 7.128 1.00 1.00 H ATOM 2920 HE2 TYR A 1158 5.152 7.853 7.423 1.00 1.00 H ATOM 2921 HE1 TYR A 1158 5.011 7.328 11.643 1.00 1.00 H ATOM 2922 HD1 TYR A 1158 6.076 5.039 11.331 1.00 1.00 H ATOM 2923 HH TYR A 1158 4.229 9.453 8.961 1.00 1.00 H ATOM 2924 HN TYR A 1158 5.103 3.351 6.854 1.00 1.00 H ATOM 2925 N SER A 1159 4.126 1.736 8.901 1.00 1.00 N ATOM 2926 CA SER A 1159 3.050 1.306 9.867 1.00 1.00 C ATOM 2927 C SER A 1159 3.532 0.234 10.847 1.00 1.00 C ATOM 2928 O SER A 1159 3.112 0.276 12.022 1.00 1.00 O ATOM 2929 CB SER A 1159 1.900 0.681 9.043 1.00 1.00 C ATOM 2930 OG SER A 1159 0.955 0.054 9.927 1.00 1.00 O ATOM 2931 HA SER A 1159 2.737 2.175 10.411 1.00 1.00 H ATOM 2932 HB1 SER A 1159 2.270 −0.076 8.309 1.00 1.00 H ATOM 2933 HB2 SER A 1159 1.416 1.452 8.527 1.00 1.00 H ATOM 2934 HG SER A 1159 0.221 −0.389 9.507 1.00 1.00 H ATOM 2935 HN SER A 1159 4.069 1.542 7.910 1.00 1.00 H ATOM 2936 CB HIE A 1160 4.117 −3.099 10.768 1.00 1.00 C ATOM 2937 CG HIE A 1160 4.124 −4.317 11.624 1.00 1.00 C ATOM 2938 ND1 HIE A 1160 4.956 −4.587 12.771 1.00 1.00 N ATOM 2939 CD2 HIE A 1160 3.396 −5.438 11.595 1.00 1.00 C ATOM 2940 CE1 HIE A 1160 4.629 −5.686 13.310 1.00 1.00 C ATOM 2941 N HIE A 1160 4.296 −0.779 10.385 1.00 1.00 N ATOM 2942 CA HIE A 1160 4.764 −1.796 11.317 1.00 1.00 C ATOM 2943 C HIE A 1160 6.255 −1.683 11.254 1.00 1.00 C ATOM 2944 O HIE A 1160 6.830 −2.629 10.714 1.00 1.00 O ATOM 2945 HB2 HIE A 1160 4.557 −3.371 9.774 1.00 1.00 H ATOM 2946 NE2 HIE A 1160 3.708 −6.240 12.583 1.00 1.00 N ATOM 2947 HB1 HIE A 1160 3.051 −2.840 10.493 1.00 1.00 H ATOM 2948 HA HIE A 1160 4.444 −1.752 12.362 1.00 1.00 H ATOM 2949 HD2 HIE A 1160 2.690 −5.691 10.834 1.00 1.00 H ATOM 2950 HE1 HIE A 1160 5.062 −6.124 14.199 1.00 1.00 H ATOM 2951 H HIE A 1160 4.535 −0.797 9.393 1.00 1.00 H ATOM 2952 HE2 HIE A 1160 3.265 −7.102 12.803 1.00 1.00 H ATOM 2953 N PRO A 1161 6.878 −0.617 11.721 1.00 1.00 N ATOM 2954 CA PRO A 1161 8.205 −0.223 11.276 1.00 1.00 C ATOM 2955 C PRO A 1161 9.034 −1.099 10.378 1.00 1.00 C ATOM 2956 O PRO A 1161 10.041 −1.609 10.812 1.00 1.00 O ATOM 2957 CB PRO A 1161 8.815 0.267 12.641 1.00 1.00 C ATOM 2958 CG PRO A 1161 7.597 0.913 13.337 1.00 1.00 C ATOM 2959 CD PRO A 1161 6.327 0.101 12.818 1.00 1.00 C ATOM 2960 HA PRO A 1161 8.147 0.686 10.627 1.00 1.00 H ATOM 2961 HD2 PRO A 1161 6.004 −0.539 13.658 1.00 1.00 H ATOM 2962 HD1 PRO A 1161 5.511 0.708 12.448 1.00 1.00 H ATOM 2963 HG2 PRO A 1161 7.706 1.032 14.432 1.00 1.00 H ATOM 2964 HG1 PRO A 1161 7.452 1.930 12.974 1.00 1.00 H ATOM 2965 HB1 PRO A 1161 9.646 1.022 12.625 1.00 1.00 H ATOM 2966 HB2 PRO A 1161 9.075 −0.599 13.268 1.00 1.00 H ATOM 2967 N ILE A 1162 8.492 −1.232 9.178 1.00 1.00 N ATOM 2968 CA ILE A 1162 9.331 −1.794 8.107 1.00 1.00 C ATOM 2969 C ILE A 1162 9.517 −0.643 7.063 1.00 1.00 C ATOM 2970 O ILE A 1162 8.550 0.090 6.779 1.00 1.00 O ATOM 2971 CB ILE A 1162 8.575 −3.048 7.512 1.00 1.00 C ATOM 2972 CG1 ILE A 1162 8.937 −4.316 8.376 1.00 1.00 C ATOM 2973 CG2 ILE A 1162 8.806 −3.205 6.008 1.00 1.00 C ATOM 2974 CD1 ILE A 1162 8.327 −5.606 7.791 1.00 1.00 C ATOM 2975 HA ILE A 1162 10.332 −2.034 8.496 1.00 1.00 H ATOM 2976 HB ILE A 1162 7.484 −2.938 7.629 1.00 1.00 H ATOM 2977 HG11 ILE A 1162 8.690 −4.246 9.429 1.00 1.00 H ATOM 2978 HG12 ILE A 1162 10.041 −4.429 8.224 1.00 1.00 H ATOM 2979 HD11 ILE A 1162 8.503 −6.402 8.489 1.00 1.00 H ATOM 2980 HD12 ILE A 1162 8.803 −5.952 6.827 1.00 1.00 H ATOM 2981 HD13 ILE A 1162 7.303 −5.531 7.508 1.00 1.00 H ATOM 2982 HG21 ILE A 1162 9.848 −3.338 5.853 1.00 1.00 H ATOM 2983 HG22 ILE A 1162 8.544 −2.271 5.530 1.00 1.00 H ATOM 2984 HG23 ILE A 1162 8.243 −4.016 5.470 1.00 1.00 H ATOM 2985 HN ILE A 1162 7.605 −0.891 8.877 1.00 1.00 H ATOM 2986 N ILE A 1163 10.738 −0.465 6.547 1.00 1.00 N ATOM 2987 CA ILE A 1163 11.014 0.720 5.697 1.00 1.00 C ATOM 2988 C ILE A 1163 11.721 0.253 4.450 1.00 1.00 C ATOM 2989 O ILE A 1163 12.775 0.651 4.061 1.00 1.00 O ATOM 2990 CB ILE A 1163 11.904 1.702 6.550 1.00 1.00 C ATOM 2991 CG1 ILE A 1163 13.188 0.985 7.060 1.00 1.00 C ATOM 2992 CG2 ILE A 1163 11.073 2.232 7.720 1.00 1.00 C ATOM 2993 CD1 ILE A 1163 14.275 1.954 7.617 1.00 1.00 C ATOM 2994 HA ILE A 1163 10.135 1.241 5.325 1.00 1.00 H ATOM 2995 HB ILE A 1163 12.159 2.543 5.885 1.00 1.00 H ATOM 2996 HG11 ILE A 1163 13.701 0.327 6.357 1.00 1.00 H ATOM 2997 HG12 ILE A 1163 12.875 0.311 7.858 1.00 1.00 H ATOM 2998 HD11 ILE A 1163 14.652 2.557 6.801 1.00 1.00 H ATOM 2999 HD12 ILE A 1163 15.123 1.296 7.956 1.00 1.00 H ATOM 3000 HD13 ILE A 1163 14.021 2.542 8.494 1.00 1.00 H ATOM 3001 HG21 ILE A 1163 10.265 2.852 7.351 1.00 1.00 H ATOM 3002 HG22 ILE A 1163 11.752 2.895 8.324 1.00 1.00 H ATOM 3003 HG23 ILE A 1163 10.673 1.425 8.335 1.00 1.00 H ATOM 3004 HN ILE A 1163 11.524 −1.071 6.724 1.00 1.00 H ATOM 3005 N LEU A 1164 11.055 −0.722 3.715 1.00 1.00 N ATOM 3006 CA LEU A 1164 11.716 −1.337 2.536 1.00 1.00 C ATOM 3007 C LEU A 1164 12.153 −0.249 1.560 1.00 1.00 C ATOM 3008 O LEU A 1164 13.360 −0.138 1.377 1.00 1.00 O ATOM 3009 CB LEU A 1164 10.820 −2.370 1.756 1.00 1.00 C ATOM 3010 CG LEU A 1164 10.336 −3.635 2.607 1.00 1.00 C ATOM 3011 CD1 LEU A 1164 9.303 −4.595 1.989 1.00 1.00 C ATOM 3012 CD2 LEU A 1164 11.516 −4.513 3.067 1.00 1.00 C ATOM 3013 HA LEU A 1164 12.599 −1.940 2.915 1.00 1.00 H ATOM 3014 HB1 LEU A 1164 9.884 −1.968 1.350 1.00 1.00 H ATOM 3015 HB2 LEU A 1164 11.389 −2.781 0.892 1.00 1.00 H ATOM 3016 HG LEU A 1164 9.869 −3.292 3.491 1.00 1.00 H ATOM 3017 HD21 LEU A 1164 11.231 −5.492 3.488 1.00 1.00 H ATOM 3018 HD22 LEU A 1164 12.107 −3.960 3.875 1.00 1.00 H ATOM 3019 HD23 LEU A 1164 12.142 −4.758 2.183 1.00 1.00 H ATOM 3020 HD11 LEU A 1164 8.983 −5.300 2.793 1.00 1.00 H ATOM 3021 HD12 LEU A 1164 9.796 −5.124 1.130 1.00 1.00 H ATOM 3022 HD13 LEU A 1164 8.478 −4.091 1.523 1.00 1.00 H ATOM 3023 HN LEU A 1164 10.234 −1.147 4.022 1.00 1.00 H ATOM 3024 N GLY A 1165 11.219 0.537 0.997 1.00 1.00 N ATOM 3025 CA GLY A 1165 11.501 1.442 −0.081 1.00 1.00 C ATOM 3026 C GLY A 1165 10.576 1.497 −1.276 1.00 1.00 C ATOM 3027 O GLY A 1165 10.674 2.392 −2.095 1.00 1.00 O ATOM 3028 HA2 GLY A 1165 12.540 1.298 −0.504 1.00 1.00 H ATOM 3029 HA1 GLY A 1165 11.423 2.417 0.327 1.00 1.00 H ATOM 3030 HN GLY A 1165 10.257 0.482 1.374 1.00 1.00 H ATOM 3031 N PHE A 1166 9.651 0.513 −1.452 1.00 1.00 N ATOM 3032 CA PHE A 1166 8.673 0.625 −2.474 1.00 1.00 C ATOM 3033 C PHE A 1166 7.432 −0.191 −2.246 1.00 1.00 C ATOM 3034 O PHE A 1166 7.608 −1.168 −1.595 1.00 1.00 O ATOM 3035 CB PHE A 1166 9.362 0.029 −3.755 1.00 1.00 C ATOM 3036 CG PHE A 1166 8.326 −0.256 −4.883 1.00 1.00 C ATOM 3037 CD1 PHE A 1166 7.643 0.785 −5.571 1.00 1.00 C ATOM 3038 CD2 PHE A 1166 8.019 −1.608 −5.280 1.00 1.00 C ATOM 3039 CE1 PHE A 1166 6.659 0.502 −6.520 1.00 1.00 C ATOM 3040 CE2 PHE A 1166 7.002 −1.864 −6.217 1.00 1.00 C ATOM 3041 CZ PHE A 1166 6.355 −0.820 −6.867 1.00 1.00 C ATOM 3042 HA PHE A 1166 8.309 1.654 −2.556 1.00 1.00 H ATOM 3043 HB1 PHE A 1166 10.057 −0.772 −3.542 1.00 1.00 H ATOM 3044 HB2 PHE A 1166 10.062 0.875 −4.068 1.00 1.00 H ATOM 3045 HD2 PHE A 1166 8.638 −2.405 −4.844 1.00 1.00 H ATOM 3046 HE2 PHE A 1166 6.722 −2.847 −6.493 1.00 1.00 H ATOM 3047 HZ PHE A 1166 5.680 −1.027 −7.621 1.00 1.00 H ATOM 3048 HE1 PHE A 1166 6.110 1.250 −7.070 1.00 1.00 H ATOM 3049 HD1 PHE A 1166 7.814 1.866 −5.413 1.00 1.00 H ATOM 3050 HN PHE A 1166 9.555 −0.261 −0.850 1.00 1.00 H ATOM 3051 N ARG A 1167 6.223 0.175 −2.711 1.00 1.00 N ATOM 3052 CA ARG A 1167 5.018 −0.721 −2.779 1.00 1.00 C ATOM 3053 C ARG A 1167 3.816 0.159 −3.052 1.00 1.00 C ATOM 3054 O ARG A 1167 3.293 0.126 −4.180 1.00 1.00 O ATOM 3055 CB ARG A 1167 4.763 −1.609 −1.520 1.00 1.00 C ATOM 3056 CG ARG A 1167 5.473 −2.994 −1.711 1.00 1.00 C ATOM 3057 CD ARG A 1167 5.895 −3.551 −0.303 1.00 1.00 C ATOM 3058 NE ARG A 1167 6.782 −4.733 −0.583 1.00 1.00 N ATOM 3059 CZ ARG A 1167 8.042 −4.620 −0.945 1.00 1.00 C ATOM 3060 NH1 ARG A 1167 8.670 −3.510 −1.162 1.00 1.00 N ATOM 3061 NH2 ARG A 1167 8.739 −5.734 −1.067 1.00 1.00 N ATOM 3062 HA ARG A 1167 5.074 −1.365 −3.664 1.00 1.00 H ATOM 3063 HB1 ARG A 1167 3.684 −1.817 −1.326 1.00 1.00 H ATOM 3064 HB2 ARG A 1167 5.131 −1.109 −0.576 1.00 1.00 H ATOM 3065 HG1 ARG A 1167 6.348 −2.908 −2.430 1.00 1.00 H ATOM 3066 HG2 ARG A 1167 4.693 −3.640 −2.192 1.00 1.00 H ATOM 3067 HD1 ARG A 1167 6.419 −2.927 0.425 1.00 1.00 H ATOM 3068 HD2 ARG A 1167 4.939 −3.815 0.183 1.00 1.00 H ATOM 3069 HE ARG A 1167 6.383 −5.638 −0.393 1.00 1.00 H ATOM 3070 HH12 ARG A 1167 9.691 −3.482 −1.363 1.00 1.00 H ATOM 3071 HH11 ARG A 1167 8.209 −2.618 −1.075 1.00 1.00 H ATOM 3072 HH22 ARG A 1167 9.726 −5.676 −1.363 1.00 1.00 H ATOM 3073 HH21 ARG A 1167 8.321 −6.639 −0.932 1.00 1.00 H ATOM 3074 HN ARG A 1167 6.131 1.018 −3.197 1.00 1.00 H ATOM 3075 N LYS A 1168 3.281 0.928 −2.076 1.00 1.00 N ATOM 3076 CA LYS A 1168 2.253 1.911 −2.360 1.00 1.00 C ATOM 3077 C LYS A 1168 3.037 3.035 −3.011 1.00 1.00 C ATOM 3078 O LYS A 1168 3.463 3.913 −2.284 1.00 1.00 O ATOM 3079 CB LYS A 1168 1.475 2.285 −1.102 1.00 1.00 C ATOM 3080 CG LYS A 1168 0.106 2.991 −1.428 1.00 1.00 C ATOM 3081 CD LYS A 1168 0.031 4.160 −2.384 1.00 1.00 C ATOM 3082 CE LYS A 1168 −1.465 4.592 −2.743 1.00 1.00 C ATOM 3083 NZ LYS A 1168 −2.334 3.454 −3.242 1.00 1.00 N ATOM 3084 HA LYS A 1168 1.553 1.556 −3.100 1.00 1.00 H ATOM 3085 HB1 LYS A 1168 2.081 2.987 −0.512 1.00 1.00 H ATOM 3086 HB2 LYS A 1168 1.369 1.404 −0.457 1.00 1.00 H ATOM 3087 HG1 LYS A 1168 −0.548 2.255 −1.820 1.00 1.00 H ATOM 3088 HG2 LYS A 1168 −0.295 3.299 −0.451 1.00 1.00 H ATOM 3089 HD1 LYS A 1168 0.501 5.018 −1.893 1.00 1.00 H ATOM 3090 HD2 LYS A 1168 0.491 3.950 −3.365 1.00 1.00 H ATOM 3091 HE1 LYS A 1168 −1.457 5.419 −3.494 1.00 1.00 H ATOM 3092 HE2 LYS A 1168 −1.865 5.025 −1.793 1.00 1.00 H ATOM 3093 HZ1 LYS A 1168 −1.872 2.865 −4.054 1.00 1.00 H ATOM 3094 HZ2 LYS A 1168 −2.746 2.731 −2.542 1.00 1.00 H ATOM 3095 HZ3 LYS A 1168 −3.346 3.762 −3.546 1.00 1.00 H ATOM 3096 HN LYS A 1168 3.622 0.917 −1.121 1.00 1.00 H ATOM 3097 N ILE A 1169 3.300 2.959 −4.356 1.00 1.00 N ATOM 3098 CA ILE A 1169 4.018 4.049 −5.018 1.00 1.00 C ATOM 3099 C ILE A 1169 3.540 5.362 −4.450 1.00 1.00 C ATOM 3100 O ILE A 1169 2.314 5.567 −4.363 1.00 1.00 O ATOM 3101 CB ILE A 1169 3.841 3.961 −6.579 1.00 1.00 C ATOM 3102 CG1 ILE A 1169 4.675 4.971 −7.397 1.00 1.00 C ATOM 3103 CG2 ILE A 1169 2.377 4.226 −6.992 1.00 1.00 C ATOM 3104 CD1 ILE A 1169 6.056 4.377 −7.688 1.00 1.00 C ATOM 3105 HA ILE A 1169 5.048 3.915 −4.745 1.00 1.00 H ATOM 3106 HB ILE A 1169 4.130 2.926 −6.782 1.00 1.00 H ATOM 3107 HG11 ILE A 1169 4.177 5.187 −8.361 1.00 1.00 H ATOM 3108 HG12 ILE A 1169 4.766 5.923 −6.815 1.00 1.00 H ATOM 3109 HD11 ILE A 1169 6.812 5.053 −8.122 1.00 1.00 H ATOM 3110 HD12 ILE A 1169 6.451 4.017 −6.729 1.00 1.00 H ATOM 3111 HD13 ILE A 1169 5.863 3.484 −8.316 1.00 1.00 H ATOM 3112 HG21 ILE A 1169 2.050 5.212 −6.785 1.00 1.00 H ATOM 3113 HG22 ILE A 1169 2.226 4.020 −8.066 1.00 1.00 H ATOM 3114 HG23 ILE A 1169 1.664 3.558 −6.460 1.00 1.00 H ATOM 3115 HN ILE A 1169 2.972 2.173 −4.927 1.00 1.00 H ATOM 3116 N PRO A 1170 4.421 6.268 −3.897 1.00 1.00 N ATOM 3117 CA PRO A 1170 3.911 7.236 −2.964 1.00 1.00 C ATOM 3118 C PRO A 1170 2.816 8.170 −3.446 1.00 1.00 C ATOM 3119 O PRO A 1170 2.575 8.228 −4.649 1.00 1.00 O ATOM 3120 CB PRO A 1170 5.195 7.907 −2.452 1.00 1.00 C ATOM 3121 CG PRO A 1170 6.296 7.468 −3.461 1.00 1.00 C ATOM 3122 CD PRO A 1170 5.891 6.082 −3.985 1.00 1.00 C ATOM 3123 HA PRO A 1170 3.514 6.682 −2.109 1.00 1.00 H ATOM 3124 HD2 PRO A 1170 6.312 5.973 −5.036 1.00 1.00 H ATOM 3125 HD1 PRO A 1170 6.229 5.253 −3.364 1.00 1.00 H ATOM 3126 HG2 PRO A 1170 7.327 7.591 −3.033 1.00 1.00 H ATOM 3127 HG1 PRO A 1170 6.314 8.266 −4.258 1.00 1.00 H ATOM 3128 HB1 PRO A 1170 5.444 7.577 −1.456 1.00 1.00 H ATOM 3129 HB2 PRO A 1170 5.091 8.986 −2.344 1.00 1.00 H ATOM 3130 N MET A 1171 2.179 8.912 −2.480 1.00 1.00 N ATOM 3131 CA MET A 1171 0.990 9.726 −2.796 1.00 1.00 C ATOM 3132 C MET A 1171 1.387 11.164 −3.139 1.00 1.00 C ATOM 3133 O MET A 1171 0.827 11.663 −4.116 1.00 1.00 O ATOM 3134 CB MET A 1171 −0.004 9.796 −1.621 1.00 1.00 C ATOM 3135 CG MET A 1171 −0.828 8.521 −1.412 1.00 1.00 C ATOM 3136 SD MET A 1171 −1.719 8.581 0.203 1.00 1.00 S ATOM 3137 CE MET A 1171 −3.145 9.684 −0.084 1.00 1.00 C ATOM 3138 HA MET A 1171 0.521 9.314 −3.719 1.00 1.00 H ATOM 3139 HB1 MET A 1171 −0.712 10.636 −1.706 1.00 1.00 H ATOM 3140 HB2 MET A 1171 0.563 10.069 −0.701 1.00 1.00 H ATOM 3141 HG1 MET A 1171 −1.462 8.441 −2.304 1.00 1.00 H ATOM 3142 HG2 MET A 1171 −0.066 7.689 −1.438 1.00 1.00 H ATOM 3143 HE1 MET A 1171 −3.724 9.329 −0.914 1.00 1.00 H ATOM 3144 HE2 MET A 1171 −3.763 9.665 0.820 1.00 1.00 H ATOM 3145 HE3 MET A 1171 2.803 10.709 −0.281 1.00 1.00 H ATOM 3146 HN MET A 1171 2.509 8.828 −1.552 1.00 1.00 H ATOM 3147 N GLY A 1172 2.329 11.774 −2.393 1.00 1.00 N ATOM 3148 CA GLY A 1172 2.668 13.164 −2.714 1.00 1.00 C ATOM 3149 C GLY A 1172 3.642 13.127 −3.845 1.00 1.00 C ATOM 3150 O GLY A 1172 4.832 13.173 −3.542 1.00 1.00 O ATOM 3151 HA2 GLY A 1172 3.179 13.683 −1.852 1.00 1.00 H ATOM 3152 HA1 GLY A 1172 1.751 13.780 −2.982 1.00 1.00 H ATOM 3153 HN GLY A 1172 2.687 11.308 −1.573 1.00 1.00 H ATOM 3154 N VAL A 1173 3.204 12.975 −5.124 1.00 1.00 N ATOM 3155 CA VAL A 1173 4.096 12.698 −6.238 1.00 1.00 C ATOM 3156 C VAL A 1173 3.342 13.296 −7.416 1.00 1.00 C ATOM 3157 O VAL A 1173 2.566 12.542 −7.993 1.00 1.00 O ATOM 3158 CB VAL A 1173 4.414 11.165 −6.434 1.00 1.00 C ATOM 3159 CG1 VAL A 1173 5.480 10.818 −7.518 1.00 1.00 C ATOM 3160 CG2 VAL A 1173 4.713 10.422 −5.122 1.00 1.00 C ATOM 3161 HA VAL A 1173 5.045 13.230 −6.077 1.00 1.00 H ATOM 3162 HB VAL A 1173 3.538 10.640 −6.830 1.00 1.00 H ATOM 3163 HG11 VAL A 1173 5.279 11.300 −8.480 1.00 1.00 H ATOM 3164 HG12 VAL A 1173 6.477 11.099 −7.196 1.00 1.00 H ATOM 3165 HG13 VAL A 1173 5.583 9.782 −7.751 1.00 1.00 H ATOM 3166 HG21 VAL A 1173 5.664 10.652 −4.660 1.00 1.00 H ATOM 3167 HG22 VAL A 1173 4.815 9.361 −5.393 1.00 1.00 H ATOM 3168 HG23 VAL A 1173 3.847 10.594 −4.437 1.00 1.00 H ATOM 3169 HN VAL A 1173 2.233 12.941 −5.343 1.00 1.00 H ATOM 3170 N GLY A 1174 3.612 14.583 −7.755 1.00 1.00 N ATOM 3171 CA GLY A 1174 2.895 15.130 −8.888 1.00 1.00 C ATOM 3172 C GLY A 1174 2.517 14.183 −9.990 1.00 1.00 C ATOM 3173 O GLY A 1174 1.408 14.146 −10.463 1.00 1.00 O ATOM 3174 HA2 GLY A 1174 3.622 15.883 −9.311 1.00 1.00 H ATOM 3175 HA1 GLY A 1174 2.007 15.668 −8.617 1.00 1.00 H ATOM 3176 HN GLY A 1174 4.223 15.158 −7.199 1.00 1.00 H ATOM 3177 N LEU A 1175 3.511 13.401 −10.479 1.00 1.00 N ATOM 3178 CA LEU A 1175 3.265 12.633 −11.697 1.00 1.00 C ATOM 3179 C LEU A 1175 2.394 11.407 −11.510 1.00 1.00 C ATOM 3180 O LEU A 1175 1.823 10.940 −12.492 1.00 1.00 O ATOM 3181 CB LEU A 1175 4.643 12.155 −12.213 1.00 1.00 C ATOM 3182 CG LEU A 1175 4.680 11.560 −13.666 1.00 1.00 C ATOM 3183 CD1 LEU A 1175 4.363 12.488 −14.906 1.00 1.00 C ATOM 3184 CD2 LEU A 1175 6.104 10.909 −13.912 1.00 1.00 C ATOM 3185 HA LEU A 1175 2.773 13.298 −12.487 1.00 1.00 H ATOM 3186 HB1 LEU A 1175 4.992 11.389 −11.464 1.00 1.00 H ATOM 3187 HB2 LEU A 1175 5.305 13.043 −12.255 1.00 1.00 H ATOM 3188 HG LEU A 1175 3.882 10.763 −13.678 1.00 1.00 H ATOM 3189 HD21 LEU A 1175 6.277 10.021 −13.225 1.00 1.00 H ATOM 3190 HD22 LEU A 1175 6.144 10.377 −14.896 1.00 1.00 H ATOM 3191 HD23 LEU A 1175 6.913 11.585 −13.857 1.00 1.00 H ATOM 3192 HD11 LEU A 1175 5.142 13.247 −15.051 1.00 1.00 H ATOM 3193 HD12 LEU A 1175 4.251 11.976 −15.875 1.00 1.00 H ATOM 3194 HD13 LEU A 1175 3.380 13.035 −14.791 1.00 1.00 H ATOM 3195 HN LEU A 1175 4.347 13.328 −9.919 1.00 1.00 H ATOM 3196 N SER A 1176 2.339 10.846 −10.264 1.00 1.00 N ATOM 3197 CA SER A 1176 1.660 9.550 −10.152 1.00 1.00 C ATOM 3198 C SER A 1176 0.217 9.484 −10.591 1.00 1.00 C ATOM 3199 O SER A 1176 −0.074 8.685 −11.460 1.00 1.00 O ATOM 3200 CB SER A 1176 1.906 8.824 −8.797 1.00 1.00 C ATOM 3201 OG SER A 1176 1.104 7.640 −8.803 1.00 1.00 O ATOM 3202 HA SER A 1176 2.180 8.815 −10.873 1.00 1.00 H ATOM 3203 HB1 SER A 1176 1.496 9.461 −7.997 1.00 1.00 H ATOM 3204 HB2 SER A 1176 3.033 8.608 −8.590 1.00 1.00 H ATOM 3205 HG SER A 1176 1.337 7.119 −8.035 1.00 1.00 H ATOM 3206 HN SER A 1176 2.777 11.263 −9.456 1.00 1.00 H ATOM 3207 N PRO A 1177 −0.745 10.235 −10.022 1.00 1.00 N ATOM 3208 CA PRO A 1177 −2.120 10.188 −10.541 1.00 1.00 C ATOM 3209 C PRO A 1177 −2.261 10.821 −11.925 1.00 1.00 C ATOM 3210 O PRO A 1177 3.320 10.640 −12.518 1.00 1.00 O ATOM 3211 CB PRO A 1177 −2.813 11.110 −9.429 1.00 1.00 C ATOM 3212 CG PRO A 1177 −1.688 12.098 −9.063 1.00 1.00 C ATOM 3213 CD PRO A 1177 −0.516 11.097 −8.876 1.00 1.00 C ATOM 3214 HA PRO A 1177 −2.484 9.178 −10.593 1.00 1.00 H ATOM 3215 HD2 PRO A 1177 0.451 11.687 −8.839 1.00 1.00 H ATOM 3216 HD1 PRO A 1177 −0.674 10.536 −7.949 1.00 1.00 H ATOM 3217 HG2 PRO A 1177 −1.946 12.562 −8.162 1.00 1.00 H ATOM 3218 HG1 PRO A 1177 −1.439 12.829 −9.865 1.00 1.00 H ATOM 3219 HB1 PRO A 1177 −3.011 10.425 −8.560 1.00 1.00 H ATOM 3220 HB2 PRO A 1177 −3.753 11.534 −9.790 1.00 1.00 H ATOM 3221 N PHE A 1178 −1.258 11.499 −12.499 1.00 1.00 N ATOM 3222 CA PHE A 1178 −1.329 12.082 −13.832 1.00 1.00 C ATOM 3223 C PHE A 1178 −1.357 11.000 −14.914 1.00 1.00 C ATOM 3224 O PHE A 1178 −2.038 11.128 −15.904 1.00 1.00 O ATOM 3225 CB PHE A 1178 −0.134 13.002 −14.118 1.00 1.00 C ATOM 3226 CG PHE A 1178 −0.299 13.873 −15.418 1.00 1.00 C ATOM 3227 CD1 PHE A 1178 0.460 13.650 −16.594 1.00 1.00 C ATOM 3228 CD2 PHE A 1178 −1.162 14.965 −15.308 1.00 1.00 C ATOM 3229 CE1 PHE A 1178 0.167 14.402 −17.701 1.00 1.00 C ATOM 3230 CE2 PHE A 1178 −1.355 15.786 −16.410 1.00 1.00 C ATOM 3231 CZ PHE A 1178 −0.695 15.488 −17.610 1.00 1.00 C ATOM 3232 HA PHE A 1178 −2.272 12.713 −13.931 1.00 1.00 H ATOM 3233 HB1 PHE A 1178 0.032 13.693 −13.257 1.00 1.00 H ATOM 3234 HB2 PHE A 1178 0.727 12.348 −14.196 1.00 1.00 H ATOM 3235 HD2 PHE A 1178 −1.614 15.188 −14.373 1.00 1.00 H ATOM 3236 HE2 PHE A 1178 −1.998 16.650 −16.267 1.00 1.00 H ATOM 3237 HZ PHE A 1178 −0.830 16.073 −18.478 1.00 1.00 H ATOM 3238 HE1 PHE A 1178 0.600 14.092 −18.620 1.00 1.00 H ATOM 3239 HD1 PHE A 1178 1.312 12.958 −16.620 1.00 1.00 H ATOM 3240 HN PHE A 1178 −0.418 11.627 −11.948 1.00 1.00 H ATOM 3241 N LEU A 1179 −0.569 9.911 −14.788 1.00 1.00 N ATOM 3242 CA LEU A 1179 −0.665 8.793 −15.707 1.00 1.00 C ATOM 3243 C LEU A 1179 −2.069 8.206 −15.512 1.00 1.00 C ATOM 3244 O LEU A 1179 −2.648 7.740 −16.479 1.00 1.00 O ATOM 3245 CB LEU A 1179 0.464 7.712 −15.544 1.00 1.00 C ATOM 3246 CG LEU A 1179 1.683 8.106 −16.406 1.00 1.00 C ATOM 3247 CD1 LEU A 1179 2.260 9.495 −15.962 1.00 1.00 C ATOM 3248 CD2 LEU A 1179 2.710 6.935 −16.407 1.00 1.00 C ATOM 3249 HA LEU A 1179 −0.660 9.082 −16.776 1.00 1.00 H ATOM 3250 HB1 LEU A 1179 0.746 7.494 −14.476 1.00 1.00 H ATOM 3251 HB2 LEU A 1179 −0.018 6.798 −15.955 1.00 1.00 H ATOM 3252 HG LEU A 1179 1.387 8.184 −17.490 1.00 1.00 H ATOM 3253 HD21 LEU A 1179 2.159 6.072 −16.828 1.00 1.00 H ATOM 3254 HD22 LEU A 1179 3.540 7.195 −17.069 1.00 1.00 H ATOM 3255 HD23 LEU A 1179 2.998 6.713 −15.406 1.00 1.00 H ATOM 3256 HD11 LEU A 1179 2.402 9.459 −14.895 1.00 1.00 H ATOM 3257 HD12 LEU A 1179 1.644 10.340 −16.215 1.00 1.00 H ATOM 3258 HD13 LEU A 1179 3.219 9.656 −16.471 1.00 1.00 H ATOM 3259 HN LEU A 1179 −0.009 9.864 −14.000 1.00 1.00 H ATOM 3260 N LEU A 1180 −2.613 8.208 −14.285 1.00 1.00 N ATOM 3261 CA LEU A 1180 −4.037 7.784 −14.174 1.00 1.00 C ATOM 3262 C LEU A 1180 −5.034 8.684 −14.899 1.00 1.00 C ATOM 3263 O LEU A 1180 −5.938 8.193 −15.557 1.00 1.00 O ATOM 3264 CB LEU A 1180 −4.534 7.537 −12.683 1.00 1.00 C ATOM 3265 CG LEU A 1180 −3.811 6.465 −11.823 1.00 1.00 C ATOM 3266 CD1 LEU A 1180 −4.282 6.358 −10.318 1.00 1.00 C ATOM 3267 CD2 LEU A 1180 −3.788 5.009 −12.430 1.00 1.00 C ATOM 3268 HA LEU A 1180 −4.072 6.837 −14.711 1.00 1.00 H ATOM 3269 HB1 LEU A 1180 −4.458 8.429 −12.040 1.00 1.00 H ATOM 3270 HB2 LEU A 1180 −5.550 7.253 −12.810 1.00 1.00 H ATOM 3271 HG LEU A 1180 −2.732 6.731 −11.855 1.00 1.00 H ATOM 3272 HD21 LEU A 1180 −3.432 5.014 −13.469 1.00 1.00 H ATOM 3273 HD22 LEU A 1180 −4.768 4.573 −12.517 1.00 1.00 H ATOM 3274 HD23 LEU A 1180 −3.090 4.266 −11.941 1.00 1.00 H ATOM 3275 HD11 LEU A 1180 −3.679 5.633 −9.826 1.00 1.00 H ATOM 3276 HD12 LEU A 1180 −5.329 6.150 −10.239 1.00 1.00 H ATOM 3277 HD13 LEU A 1180 −4.110 7.309 −9.810 1.00 1.00 H ATOM 3278 HN LEU A 1180 −2.102 8.439 −13.414 1.00 1.00 H ATOM 3279 N ALA A 1181 −4.891 10.018 −14.689 1.00 1.00 N ATOM 3280 CA ALA A 1181 −5.698 10.967 −15.460 1.00 1.00 C ATOM 3281 C ALA A 1181 −5.498 10.776 −16.983 1.00 1.00 C ATOM 3282 O ALA A 1181 −6.493 10.675 −17.702 1.00 1.00 O ATOM 3283 CB ALA A 1181 −5.324 12.459 −15.130 1.00 1.00 C ATOM 3284 HA ALA A 1181 −6.724 10.795 −15.240 1.00 1.00 H ATOM 3285 HB1 ALA A 1181 −5.562 12.531 −14.062 1.00 1.00 H ATOM 3286 HB2 ALA A 1181 −4.276 12.759 −15.337 1.00 1.00 H ATOM 3287 HB3 ALA A 1181 −6.001 13.098 −15.681 1.00 1.00 H ATOM 3288 HN ALA A 1181 −4.148 10.358 −14.143 1.00 1.00 H ATOM 3289 N GLN A 1182 −4.236 10.767 −17.521 1.00 1.00 N ATOM 3290 CA GLN A 1182 −4.072 10.684 −18.980 1.00 1.00 C ATOM 3291 C GLN A 1182 −4.770 9.404 −19.366 1.00 1.00 C ATOM 3292 O GLN A 1182 −5.570 9.338 −20.286 1.00 1.00 O ATOM 3293 CB GLN A 1182 −2.595 10.644 −19.394 1.00 1.00 C ATOM 3294 CG GLN A 1182 −1.900 12.036 −19.233 1.00 1.00 C ATOM 3295 CD GLN A 1182 −0.420 11.888 −19.533 1.00 1.00 C ATOM 3296 OE1 GLN A 1182 0.256 11.016 −19.029 1.00 1.00 O ATOM 3297 NE2 GLN A 1182 0.145 12.691 −20.456 1.00 1.00 N ATOM 3298 HA GLN A 1182 −4.593 11.604 −19.352 1.00 1.00 H ATOM 3299 HB1 GLN A 1182 −2.577 10.511 −20.482 1.00 1.00 H ATOM 3300 HB2 GLN A 1182 −2.100 9.845 −18.806 1.00 1.00 H ATOM 3301 HG1 GLN A 1182 −2.302 12.787 −19.978 1.00 1.00 H ATOM 3302 HG2 GLN A 1182 −1.942 12.444 −18.235 1.00 1.00 H ATOM 3303 HE22 GLN A 1182 1.074 12.556 −20.747 1.00 1.00 H ATOM 3304 HE21 GLN A 1182 −0.324 13.479 −20.830 1.00 1.00 H ATOM 3305 HN GLN A 1182 −3.486 10.925 −16.924 1.00 1.00 H ATOM 3306 N PHE A 1183 −4.399 8.287 −18.665 1.00 1.00 N ATOM 3307 CA PHE A 1183 −5.062 6.974 −18.909 1.00 1.00 C ATOM 3308 C PHE A 1183 −6.541 7.137 −18.907 1.00 1.00 C ATOM 3309 O PHE A 1183 −7.202 6.566 −19.764 1.00 1.00 O ATOM 3310 CB PHE A 1183 −4.538 5.902 −17.902 1.00 1.00 C ATOM 3311 CG PHE A 1183 −5.395 4.618 −17.982 1.00 1.00 C ATOM 3312 CD1 PHE A 1183 −6.258 4.282 −16.943 1.00 1.00 C ATOM 3313 CD2 PHE A 1183 −5.276 3.769 −19.099 1.00 1.00 C ATOM 3314 CE1 PHE A 1183 −7.031 3.094 −17.033 1.00 1.00 C ATOM 3315 CE2 PHE A 1183 −5.950 2.566 −19.142 1.00 1.00 C ATOM 3316 CZ PHE A 1183 −6.880 2.260 −18.124 1.00 1.00 C ATOM 3317 HA PHE A 1183 −4.771 6.684 −19.899 1.00 1.00 H ATOM 3318 HB1 PHE A 1183 −4.724 6.417 −16.942 1.00 1.00 H ATOM 3319 HB2 PHE A 1183 −3.450 5.623 −17.993 1.00 1.00 H ATOM 3320 HD2 PHE A 1183 −4.615 4.162 −19.891 1.00 1.00 H ATOM 3321 HE2 PHE A 1183 −5.766 1.920 −19.960 1.00 1.00 H ATOM 3322 HZ PHE A 1183 −7.530 1.416 −18.276 1.00 1.00 H ATOM 3323 HE1 PHE A 1183 −7.689 2.776 −16.268 1.00 1.00 H ATOM 3324 HD1 PHE A 1183 −6.334 4.896 −16.052 1.00 1.00 H ATOM 3325 HN PHE A 1183 −3.714 8.346 −17.953 1.00 1.00 H ATOM 3326 N THR A 1184 −7.206 7.838 −17.954 1.00 1.00 N ATOM 3327 CA THR A 1184 −8.657 7.971 −18.080 1.00 1.00 C ATOM 3328 C THR A 1184 −8.894 8.636 −19.451 1.00 1.00 C ATOM 3329 O THR A 1184 −9.716 8.064 −20.128 1.00 1.00 O ATOM 3330 CB THR A 1184 −9.194 8.817 −16.920 1.00 1.00 C ATOM 3331 OG1 THR A 1184 −8.664 8.195 −15.711 1.00 1.00 O ATOM 3332 CG2 THR A 1184 −10.727 8.690 −16.781 1.00 1.00 C ATOM 3333 HA THR A 1184 −9.062 6.947 −18.125 1.00 1.00 H ATOM 3334 HB THR A 1184 −8.876 9.814 −16.974 1.00 1.00 H ATOM 3335 HG1 THR A 1184 −8.924 8.523 −14.865 1.00 1.00 H ATOM 3336 HG23 THR A 1184 −11.203 9.157 −17.692 1.00 1.00 H ATOM 3337 HG21 THR A 1184 −11.028 7.646 −16.673 1.00 1.00 H ATOM 3338 HG22 THR A 1184 −11.152 9.189 −15.886 1.00 1.00 H ATOM 3339 HN THR A 1184 −6.686 8.304 −17.178 1.00 1.00 H ATOM 3340 N SER A 1185 −8.197 9.701 −19.929 1.00 1.00 N ATOM 3341 CA SER A 1185 −8.305 10.134 −21.329 1.00 1.00 C ATOM 3342 C SER A 1185 −8.169 8.924 −22.214 1.00 1.00 C ATOM 3343 O SER A 1185 −8.959 8.780 −23.130 1.00 1.00 O ATOM 3344 CB SER A 1185 −7.374 11.293 −21.780 1.00 1.00 C ATOM 3345 OG SER A 1185 −7.759 11.902 −23.026 1.00 1.00 O ATOM 3346 HA SER A 1185 −9.290 10.592 −21.405 1.00 1.00 H ATOM 3347 HB1 SER A 1185 −6.338 10.918 −21.845 1.00 1.00 H ATOM 3348 HB2 SER A 1185 −7.420 12.054 −20.980 1.00 1.00 H ATOM 3349 HG SER A 1185 −7.701 11.226 −23.703 1.00 1.00 H ATOM 3350 HN SER A 1185 −7.517 10.113 −19.342 1.00 1.00 H ATOM 3351 N ALA A 1186 −7.164 8.065 −22.049 1.00 1.00 N ATOM 3352 CA ALA A 1186 −7.202 6.908 −22.915 1.00 1.00 C ATOM 3353 C ALA A 1186 −8.516 6.123 −22.766 1.00 1.00 C ATOM 3354 O ALA A 1186 −8.882 5.571 −23.815 1.00 1.00 O ATOM 3355 CB ALA A 1186 −5.896 6.083 −22.759 1.00 1.00 C ATOM 3356 HA ALA A 1186 −7.242 7.260 −24.002 1.00 1.00 H ATOM 3357 HB1 ALA A 1186 −5.760 5.404 −23.603 1.00 1.00 H ATOM 3358 HB2 ALA A 1186 −5.046 6.762 −22.634 1.00 1.00 H ATOM 3359 HB3 ALA A 1186 −6.003 5.552 −21.816 1.00 1.00 H ATOM 3360 HN ALA A 1186 −6.532 8.152 −21.311 1.00 1.00 H ATOM 3361 N ILE A 1187 −9.211 6.080 −21.634 1.00 1.00 N ATOM 3362 CA ILE A 1187 −10.563 5.485 −21.655 1.00 1.00 C ATOM 3363 C ILE A 1187 −11.561 6.268 −22.453 1.00 1.00 C ATOM 3364 O ILE A 1187 −12.392 5.691 −23.134 1.00 1.00 O ATOM 3365 CB ILE A 1187 −11.103 5.086 −20.269 1.00 1.00 C ATOM 3366 CG1 ILE A 1187 −10.144 4.114 −19.474 1.00 1.00 C ATOM 3367 CG2 ILE A 1187 −12.516 4.434 −20.397 1.00 1.00 C ATOM 3368 CD1 ILE A 1187 −9.448 2.959 −20.316 1.00 1.00 C ATOM 3369 HA ILE A 1187 −10.469 4.606 −22.238 1.00 1.00 H ATOM 3370 HB ILE A 1187 −11.290 5.966 −19.643 1.00 1.00 H ATOM 3371 HG11 ILE A 1187 −9.312 4.745 −19.122 1.00 1.00 H ATOM 3372 HG12 ILE A 1187 −10.591 3.726 −18.568 1.00 1.00 H ATOM 3373 HD11 ILE A 1187 −10.181 2.383 −20.916 1.00 1.00 H ATOM 3374 HD12 ILE A 1187 −8.615 3.404 −20.925 1.00 1.00 H ATOM 3375 HD13 ILE A 1187 −9.011 2.278 −19.608 1.00 1.00 H ATOM 3376 HG21 ILE A 1187 −12.527 3.643 −21.168 1.00 1.00 H ATOM 3377 HG22 ILE A 1187 −12.847 3.922 −19.424 1.00 1.00 H ATOM 3378 HG23 ILE A 1187 −13.271 5.202 −20.697 1.00 1.00 H ATOM 3379 HN ILE A 1187 −8.848 6.524 −20.804 1.00 1.00 H ATOM 3380 N CYS A 1188 −11.446 7.611 −22.353 1.00 1.00 N ATOM 3381 CA CYS A 1188 −12.216 8.460 −23.238 1.00 1.00 C ATOM 3382 C CYS A 1188 −12.107 7.883 −24.603 1.00 1.00 C ATOM 3383 O CYS A 1188 −13.097 7.644 −25.280 1.00 1.00 O ATOM 3384 CB CYS A 1188 −11.623 9.879 −23.343 1.00 1.00 C ATOM 3385 SG CYS A 1188 −12.756 11.068 −24.162 1.00 1.00 S ATOM 3386 HA CYS A 1188 −13.264 8.490 −22.934 1.00 1.00 H ATOM 3387 HB1 CYS A 1188 −11.440 10.249 −22.315 1.00 1.00 H ATOM 3388 HB2 CYS A 1188 −10.671 9.976 −23.923 1.00 1.00 H ATOM 3389 HG CYS A 1188 −12.108 11.830 −24.258 1.00 1.00 H ATOM 3390 HN CYS A 1188 −10.808 7.988 −21.671 1.00 1.00 H ATOM 3391 N SER A 1189 −10.835 7.543 −25.027 1.00 1.00 N ATOM 3392 CA SER A 1189 −10.685 7.039 −26.408 1.00 1.00 C ATOM 3393 C SER A 1189 −11.465 5.739 −26.573 1.00 1.00 C ATOM 3394 O SER A 1189 −12.279 5.676 −27.495 1.00 1.00 O ATOM 3395 CB SER A 1189 −9.198 6.815 −26.826 1.00 1.00 C ATOM 3396 OG SER A 1189 −8.501 5.670 −26.365 1.00 1.00 O ATOM 3397 HA SER A 1189 −11.134 7.804 −27.138 1.00 1.00 H ATOM 3398 HB1 SER A 1189 −9.173 6.636 −27.942 1.00 1.00 H ATOM 3399 HB2 SER A 1189 −8.638 7.705 −26.512 1.00 1.00 H ATOM 3400 HG SER A 1189 −8.375 5.667 −25.431 1.00 1.00 H ATOM 3401 HN SER A 1189 −9.975 7.671 −24.485 1.00 1.00 H ATOM 3402 N VAL A 1190 −11.185 4.677 −25.795 1.00 1.00 N ATOM 3403 CA VAL A 1190 −11.822 3.361 −26.161 1.00 1.00 C ATOM 3404 C VAL A 1190 −13.394 3.508 −25.977 1.00 1.00 C ATOM 3405 O VAL A 1190 −14.209 2.963 −26.739 1.00 1.00 O ATOM 3406 CB VAL A 1190 −11.165 2.069 −25.530 1.00 1.00 C ATOM 3407 CG1 VAL A 1190 −9.678 1.848 −25.884 1.00 1.00 C ATOM 3408 CG2 VAL A 1190 −11.343 1.874 −24.045 1.00 1.00 C ATOM 3409 HA VAL A 1190 −11.695 3.271 −27.259 1.00 1.00 H ATOM 3410 HB VAL A 1190 −11.687 1.228 −25.938 1.00 1.00 H ATOM 3411 HG11 VAL A 1190 −9.091 2.637 −25.395 1.00 1.00 H ATOM 3412 HG12 VAL A 1190 −9.482 1.923 −26.980 1.00 1.00 H ATOM 3413 HG13 VAL A 1190 −9.270 0.885 −25.560 1.00 1.00 H ATOM 3414 HG21 VAL A 1190 −11.063 0.864 −23.686 1.00 1.00 H ATOM 3415 HG22 VAL A 1190 −10.704 2.616 −23.553 1.00 1.00 H ATOM 3416 HG23 VAL A 1190 −12.401 2.094 −23.724 1.00 1.00 H ATOM 3417 HN VAL A 1190 −10.519 4.707 −25.008 1.00 1.00 H ATOM 3418 N VAL A 1191 −13.827 4.243 −24.916 1.00 1.00 N ATOM 3419 CA VAL A 1191 −15.254 4.468 −24.789 1.00 1.00 C ATOM 3420 C VAL A 1191 −15.897 5.198 −25.961 1.00 1.00 C ATOM 3421 O VAL A 1191 −16.947 4.782 −26.497 1.00 1.00 O ATOM 3422 CB VAL A 1191 −15.551 5.099 −23.406 1.00 1.00 C ATOM 3423 CG1 VAL A 1191 −16.936 5.890 −23.317 1.00 1.00 C ATOM 3424 CG2 VAL A 1191 −15.495 3.988 −22.317 1.00 1.00 C ATOM 3425 HA VAL A 1191 −15.850 3.558 −24.721 1.00 1.00 H ATOM 3426 HB VAL A 1191 −14.794 5.912 −23.161 1.00 1.00 H ATOM 3427 HG11 VAL A 1191 −16.824 6.849 −23.917 1.00 1.00 H ATOM 3428 HG12 VAL A 1191 −17.774 5.331 −23.736 1.00 1.00 H ATOM 3429 HG13 VAL A 1191 −17.190 6.153 −22.291 1.00 1.00 H ATOM 3430 HG21 VAL A 1191 −16.396 3.364 −22.416 1.00 1.00 H ATOM 3431 HG22 VAL A 1191 −14.646 3.289 −22.345 1.00 1.00 H ATOM 3432 HG23 VAL A 1191 −15.513 4.452 −21.330 1.00 1.00 H ATOM 3433 HN VAL A 1191 −13.191 4.551 −24.226 1.00 1.00 H ATOM 3434 N ARG A 1192 −15.250 6.282 −26.470 1.00 1.00 N ATOM 3435 CA ARG A 1192 −15.726 6.827 −27.730 1.00 1.00 C ATOM 3436 C ARG A 1192 −15.679 5.712 −28.759 1.00 1.00 C ATOM 3437 O ARG A 1192 −16.673 5.468 −29.428 1.00 1.00 O ATOM 3438 CB ARG A 1192 −14.873 8.047 −28.215 1.00 1.00 C ATOM 3439 CG ARG A 1192 −15.549 9.379 −27.669 1.00 1.00 C ATOM 3440 CD ARG A 1192 −15.695 9.449 −26.156 1.00 1.00 C ATOM 3441 NE ARG A 1192 −16.339 10.708 −25.746 1.00 1.00 N ATOM 3442 CZ ARG A 1192 −16.450 11.075 −24.490 1.00 1.00 C ATOM 3443 NH1 ARG A 1192 −15.995 10.342 −23.494 1.00 1.00 N ATOM 3444 NH2 ARG A 1192 −17.078 12.235 −24.233 1.00 1.00 N ATOM 3445 HA ARG A 1192 −16.798 7.060 −27.583 1.00 1.00 H ATOM 3446 HB1 ARG A 1192 −14.922 8.121 −29.308 1.00 1.00 H ATOM 3447 HB2 ARG A 1192 −13.848 7.987 −27.883 1.00 1.00 H ATOM 3448 HG1 ARG A 1192 −14.915 10.220 −28.088 1.00 1.00 H ATOM 3449 HG2 ARG A 1192 −16.535 9.521 −28.086 1.00 1.00 H ATOM 3450 HD1 ARG A 1192 −16.335 8.652 −25.819 1.00 1.00 H ATOM 3451 HD2 ARG A 1192 −14.694 9.230 −25.763 1.00 1.00 H ATOM 3452 HE ARG A 1192 −16.697 11.317 −26.474 1.00 1.00 H ATOM 3453 HH12 ARG A 1192 −16.032 10.720 −22.511 1.00 1.00 H ATOM 3454 HH11 ARG A 1192 −15.539 9.450 −23.619 1.00 1.00 H ATOM 3455 HH22 ARG A 1192 −17.255 12.515 −23.248 1.00 1.00 H ATOM 3456 HH21 ARG A 1192 −17.466 12.806 −24.972 1.00 1.00 H ATOM 3457 HN ARG A 1192 −14.416 6.686 −26.038 1.00 1.00 H ATOM 3458 N ARG A 1193 −14.568 4.990 −28.979 1.00 1.00 N ATOM 3459 CA ARG A 1193 −14.596 3.880 −29.899 1.00 1.00 C ATOM 3460 C ARG A 1193 −15.880 3.087 −29.744 1.00 1.00 C ATOM 3461 O ARG A 1193 −16.593 2.807 −30.694 1.00 1.00 O ATOM 3462 CB ARG A 1193 −13.390 2.965 −29.795 1.00 1.00 C ATOM 3463 CG ARG A 1193 −13.343 1.980 −31.031 1.00 1.00 C ATOM 3464 CD ARG A 1193 −14.035 0.557 −30.871 1.00 1.00 C ATOM 3465 NE ARG A 1193 −13.357 −0.155 −29.803 1.00 1.00 N ATOM 3466 CZ ARG A 1193 −13.643 −1.376 −29.408 1.00 1.00 C ATOM 3467 NH1 ARG A 1193 −14.612 −2.083 −29.853 1.00 1.00 N ATOM 3468 NH2 ARG A 1193 −12.936 −1.832 −28.418 1.00 1.00 N ATOM 3469 HA ARG A 1193 −14.545 4.332 −30.868 1.00 1.00 H ATOM 3470 HB1 ARG A 1193 −13.376 2.389 −28.841 1.00 1.00 H ATOM 3471 HB2 ARG A 1193 −12.478 3.556 −29.845 1.00 1.00 H ATOM 3472 HG1 ARG A 1193 −13.751 2.467 −31.935 1.00 1.00 H ATOM 3473 HG2 ARG A 1193 −12.306 1.702 −31.354 1.00 1.00 H ATOM 3474 HD1 ARG A 1193 −15.089 0.762 −30.678 1.00 1.00 H ATOM 3475 HD2 ARG A 1193 −13.982 0.105 −31.883 1.00 1.00 H ATOM 3476 HE ARG A 1193 −12.508 0.319 −29.393 1.00 1.00 H ATOM 3477 HH12 ARG A 1193 −14.756 −3.062 −29.561 1.00 1.00 H ATOM 3478 HH11 ARG A 1193 −15.241 −1.746 −30.595 1.00 1.00 H ATOM 3479 HH22 ARG A 1193 −13.075 −2.780 −28.063 1.00 1.00 H ATOM 3480 HH21 ARG A 1193 −12.175 −1.345 −27.983 1.00 1.00 H ATOM 3481 HN ARG A 1193 −13.773 5.114 −28.364 1.00 1.00 H ATOM 3482 N ALA A 1194 −16.257 2.756 −28.480 1.00 1.00 N ATOM 3483 CA ALA A 1194 −17.617 2.074 −28.302 1.00 1.00 C ATOM 3484 C ALA A 1194 −17.498 0.563 −28.547 1.00 1.00 C ATOM 3485 O ALA A 1194 −16.460 0.073 −28.977 1.00 1.00 O ATOM 3486 CB ALA A 1194 −18.799 2.646 −29.140 1.00 1.00 C ATOM 3487 HA ALA A 1194 −17.873 2.269 −27.238 1.00 1.00 H ATOM 3488 HB1 ALA A 1194 −18.869 2.258 −30.180 1.00 1.00 H ATOM 3489 HB2 ALA A 1194 −19.813 2.425 −28.651 1.00 1.00 H ATOM 3490 HB3 ALA A 1194 −18.732 3.737 −29.285 1.00 1.00 H ATOM 3491 HN ALA A 1194 −15.703 2.951 −27.674 1.00 1.00 H ATOM 3492 N PHE A 1195 −18.560 −0.261 −28.214 1.00 1.00 N ATOM 3493 CA PHE A 1195 −18.399 −1.706 −28.289 1.00 1.00 C ATOM 3494 C PHE A 1195 −19.735 −2.324 −28.776 1.00 1.00 C ATOM 3495 O PHE A 1195 −20.682 −1.545 −28.741 1.00 1.00 O ATOM 3496 CB PHE A 1195 −17.977 −2.282 −26.922 1.00 1.00 C ATOM 3497 CG PHE A 1195 −16.938 −1.333 −26.221 1.00 1.00 C ATOM 3498 CD1 PHE A 1195 −15.573 −1.523 −26.421 1.00 1.00 C ATOM 3499 CD2 PHE A 1195 −17.383 −0.307 −25.358 1.00 1.00 C ATOM 3500 CE1 PHE A 1195 −14.668 −0.618 −25.868 1.00 1.00 C ATOM 3501 CE2 PHE A 1195 −16.484 0.598 −24.792 1.00 1.00 C ATOM 3502 CZ PHE A 1195 −15.110 0.400 −25.046 1.00 1.00 C ATOM 3503 HA PHE A 1195 −17.661 −1.974 −29.031 1.00 1.00 H ATOM 3504 HB1 PHE A 1195 −17.478 −3.255 −27.117 1.00 1.00 H ATOM 3505 HB2 PHE A 1195 −18.850 −2.480 −26.238 1.00 1.00 H ATOM 3506 HD2 PHE A 1195 −18.462 −0.175 −25.256 1.00 1.00 H ATOM 3507 HE2 PHE A 1195 −16.800 1.401 −24.164 1.00 1.00 H ATOM 3508 HZ PHE A 1195 −14.384 1.013 −24.458 1.00 1.00 H ATOM 3509 HE1 PHE A 1195 −13.607 −0.660 −26.032 1.00 1.00 H ATOM 3510 HD1 PHE A 1195 −15.190 −2.423 −26.968 1.00 1.00 H ATOM 3511 HN PHE A 1195 −19.436 0.091 −27.783 1.00 1.00 H ATOM 3512 N PRO A 1196 −19.889 −3.623 −29.149 1.00 1.00 N ATOM 3513 CA PRO A 1196 −21.176 −4.038 −29.691 1.00 1.00 C ATOM 3514 C PRO A 1196 −22.305 −3.987 −28.726 1.00 1.00 C ATOM 3515 O PRO A 1196 −23.396 −3.572 −29.083 1.00 1.00 O ATOM 3516 CB PRO A 1196 −20.820 −5.541 −30.052 1.00 1.00 C ATOM 3517 CG PRO A 1196 −19.308 −5.478 −30.296 1.00 1.00 C ATOM 3518 CD PRO A 1196 −18.794 −4.545 −29.200 1.00 1.00 C ATOM 3519 HA PRO A 1196 −21.426 −3.486 −30.561 1.00 1.00 H ATOM 3520 HD2 PRO A 1196 −18.611 −5.023 −28.224 1.00 1.00 H ATOM 3521 HD1 PRO A 1196 −17.794 −4.228 −29.613 1.00 1.00 H ATOM 3522 HG2 PRO A 1196 −19.207 −4.978 −31.293 1.00 1.00 H ATOM 3523 HG1 PRO A 1196 −18.826 −6.457 −30.257 1.00 1.00 H ATOM 3524 HB1 PRO A 1196 −21.382 −5.871 −30.949 1.00 1.00 H ATOM 3525 HB2 PRO A 1196 −21.036 −6.220 −29.237 1.00 1.00 H ATOM 3526 N HIE A 1197 −22.078 −4.442 −27.474 1.00 1.00 N ATOM 3527 CA HIE A 1197 −23.163 −4.316 −26.461 1.00 1.00 C ATOM 3528 C HIE A 1197 −22.525 −4.223 −25.102 1.00 1.00 C ATOM 3529 O HIE A 1197 −23.027 −4.857 −24.182 1.00 1.00 O ATOM 3530 H HIE A 1197 −21.171 −4.796 −27.220 1.00 1.00 H ATOM 3531 CB HIE A 1197 −24.141 −5.461 −26.532 1.00 1.00 C ATOM 3532 HB2 HIE A 1197 −24.570 −5.524 −27.564 1.00 1.00 H ATOM 3533 CG HIE A 1197 −23.424 −6.734 −26.316 1.00 1.00 C ATOM 3534 ND1 HIE A 1197 −23.250 −7.356 −25.037 1.00 1.00 N ATOM 3535 CD2 HIE A 1197 −22.820 −7.582 −27.164 1.00 1.00 C ATOM 3536 HA HIE A 1197 −23.747 −3.431 −26.668 1.00 1.00 H ATOM 3537 CE1 HIE A 1197 −22.502 −8.388 −25.196 1.00 1.00 C ATOM 3538 NE2 HIE A 1197 −22.223 −8.522 −26.448 1.00 1.00 N ATOM 3539 HB1 HIE A 1197 −25.035 −5.359 −25.845 1.00 1.00 H ATOM 3540 HD2 HIE A 1197 −22.734 −7.423 −28.264 1.00 1.00 H ATOM 3541 HE1 HIE A 1197 −22.213 −9.064 −24.447 1.00 1.00 H ATOM 3542 HE2 HIE A 1197 −21.625 −9.305 −26.817 1.00 1.00 H ATOM 3543 N CYS A 1198 −21.375 −3.527 −24.896 1.00 1.00 N ATOM 3544 CA CYS A 1198 −20.612 −3.835 −23.683 1.00 1.00 C ATOM 3545 C CYS A 1198 −19.834 −2.604 −23.272 1.00 1.00 C ATOM 3546 O CYS A 1198 −18.658 −2.432 −23.519 1.00 1.00 O ATOM 3547 CB CYS A 1198 −19.579 −4.959 −23.925 1.00 1.00 C ATOM 3548 SG CYS A 1198 −20.399 −6.526 −24.173 1.00 1.00 S ATOM 3549 HA CYS A 1198 −21.265 −4.089 −22.839 1.00 1.00 H ATOM 3550 HB1 CYS A 1198 −18.900 −4.851 −24.759 1.00 1.00 H ATOM 3551 HB2 CYS A 1198 −18.995 −5.076 −23.013 1.00 1.00 H ATOM 3552 HG CYS A 1198 −19.595 −7.081 −24.483 1.00 1.00 H ATOM 3553 HN CYS A 1198 −21.041 −2.893 −25.587 1.00 1.00 H ATOM 3554 N LEU A 1199 −20.546 −1.672 −22.546 1.00 1.00 N ATOM 3555 CA LEU A 1199 −19.927 −0.417 −22.072 1.00 1.00 C ATOM 3556 C LEU A 1199 −19.363 −0.595 −20.665 1.00 1.00 C ATOM 3557 O LEU A 1199 −19.752 −1.550 −20.030 1.00 1.00 O ATOM 3558 CB LEU A 1199 −21.069 0.679 −22.196 1.00 1.00 C ATOM 3559 CG LEU A 1199 −20.728 2.186 −21.929 1.00 1.00 C ATOM 3560 CD1 LEU A 1199 −19.671 2.733 −22.942 1.00 1.00 C ATOM 3561 CD2 LEU A 1199 −22.051 2.988 −22.149 1.00 1.00 C ATOM 3562 HA LEU A 1199 −19.044 −0.102 −22.683 1.00 1.00 H ATOM 3563 HB1 LEU A 1199 −21.956 0.405 −21.562 1.00 1.00 H ATOM 3564 HB2 LEU A 1199 −21.378 0.575 −23.277 1.00 1.00 H ATOM 3565 HG LEU A 1199 −20.299 2.407 −20.937 1.00 1.00 H ATOM 3566 HD21 LEU A 1199 −22.429 2.870 −23.193 1.00 1.00 H ATOM 3567 HD22 LEU A 1199 −22.856 2.688 −21.456 1.00 1.00 H ATOM 3568 HD23 LEU A 1199 −21.815 4.092 −22.004 1.00 1.00 H ATOM 3569 HD11 LEU A 1199 −18.670 2.336 −22.709 1.00 1.00 H ATOM 3570 HD12 LEU A 1199 −20.004 2.447 −23.915 1.00 1.00 H ATOM 3571 HD13 LEU A 1199 −19.575 3.821 −23.029 1.00 1.00 H ATOM 3572 HN LEU A 1199 −21.514 −1.853 −22.370 1.00 1.00 H ATOM 3573 N ALA A 1200 −18.508 0.358 −20.172 1.00 1.00 N ATOM 3574 CA ALA A 1200 −17.935 0.285 −18.812 1.00 1.00 C ATOM 3575 C ALA A 1200 −17.362 1.605 −18.373 1.00 1.00 C ATOM 3576 O ALA A 1200 −17.255 2.446 −19.209 1.00 1.00 O ATOM 3577 CB ALA A 1200 −16.882 −0.845 −18.951 1.00 1.00 C ATOM 3578 HA ALA A 1200 −18.705 0.058 −18.072 1.00 1.00 H ATOM 3579 HB1 ALA A 1200 −17.264 −1.761 −19.432 1.00 1.00 H ATOM 3580 HB2 ALA A 1200 −16.063 −0.387 −19.533 1.00 1.00 H ATOM 3581 HB3 ALA A 1200 −16.439 −1.125 −17.944 1.00 1.00 H ATOM 3582 HN ALA A 1200 −18.212 1.152 −20.718 1.00 1.00 H ATOM 3583 N PHE A 1201 −16.915 1.804 −17.136 1.00 1.00 N ATOM 3584 CA PHE A 1201 −16.267 3.080 −16.850 1.00 1.00 C ATOM 3585 C PHE A 1201 −15.223 3.098 −15.749 1.00 1.00 C ATOM 3586 O PHE A 1201 −15.128 2.054 −15.148 1.00 1.00 O ATOM 3587 CB PHE A 1201 −17.316 4.155 −16.454 1.00 1.00 C ATOM 3588 CG PHE A 1201 −18.303 4.433 −17.577 1.00 1.00 C ATOM 3589 CD1 PHE A 1201 −19.578 3.908 −17.584 1.00 1.00 C ATOM 3590 CD2 PHE A 1201 −17.953 5.341 −18.565 1.00 1.00 C ATOM 3591 CE1 PHE A 1201 −20.545 4.446 −18.433 1.00 1.00 C ATOM 3592 CE2 PHE A 1201 −18.895 5.832 −19.470 1.00 1.00 C ATOM 3593 CZ PHE A 1201 −20.224 5.416 −19.378 1.00 1.00 C ATOM 3594 HA PHE A 1201 −15.733 3.356 −17.734 1.00 1.00 H ATOM 3595 HB1 PHE A 1201 −16.872 5.092 −16.152 1.00 1.00 H ATOM 3596 HB2 PHE A 1201 −17.944 3.787 −15.586 1.00 1.00 H ATOM 3597 HD2 PHE A 1201 −16.909 5.710 −18.596 1.00 1.00 H ATOM 3598 HE2 PHE A 1201 −18.657 6.564 −20.245 1.00 1.00 H ATOM 3599 HZ PHE A 1201 −20.973 5.730 −20.071 1.00 1.00 H ATOM 3600 HE1 PHE A 1201 −21.567 4.033 −18.444 1.00 1.00 H ATOM 3601 HD1 PHE A 1201 −19.861 3.123 −16.898 1.00 1.00 H ATOM 3602 HN PHE A 1201 −16.914 1.057 −16.481 1.00 1.00 H ATOM 3603 N SER A 1202 −14.438 4.188 −15.677 1.00 1.00 N ATOM 3604 CA SER A 1202 −13.332 4.241 −14.674 1.00 1.00 C ATOM 3605 C SER A 1202 −12.951 5.596 −14.067 1.00 1.00 C ATOM 3606 O SER A 1202 −13.123 6.592 −14.762 1.00 1.00 O ATOM 3607 CB SER A 1202 −12.054 3.592 −15.239 1.00 1.00 C ATOM 3608 OG SER A 1202 −11.574 4.218 −16.422 1.00 1.00 O ATOM 3609 HA SER A 1202 −13.644 3.666 −13.783 1.00 1.00 H ATOM 3610 HB1 SER A 1202 −12.310 2.549 −15.484 1.00 1.00 H ATOM 3611 HB2 SER A 1202 −11.225 3.618 −14.542 1.00 1.00 H ATOM 3612 HG SER A 1202 −11.198 5.049 −16.215 1.00 1.00 H ATOM 3613 HN SER A 1202 −14.535 4.896 −16.380 1.00 1.00 H ATOM 3614 N TYR A 1203 −12.471 5.610 −12.807 1.00 1.00 N ATOM 3615 CA TYR A 1203 −12.058 6.860 −12.104 1.00 1.00 C ATOM 3616 C TYR A 1203 −10.901 6.554 −11.119 1.00 1.00 C ATOM 3617 O TYR A 1203 −11.206 6.213 −10.025 1.00 1.00 O ATOM 3618 CB TYR A 1203 −13.288 7.487 −11.427 1.00 1.00 C ATOM 3619 CG TYR A 1203 −13.038 8.955 −11.074 1.00 1.00 C ATOM 3620 CD1 TYR A 1203 −13.544 10.001 −11.838 1.00 1.00 C ATOM 3621 CD2 TYR A 1203 −12.283 9.319 −9.944 1.00 1.00 C ATOM 3622 CE1 TYR A 1203 −13.382 11.334 −11.478 1.00 1.00 C ATOM 3623 CE2 TYR A 1203 −12.037 10.668 −9.601 1.00 1.00 C ATOM 3624 CZ TYR A 1203 −12.682 11.647 −10.342 1.00 1.00 C ATOM 3625 OH TYR A 1203 −12.600 12.962 −9.950 1.00 1.00 O ATOM 3626 HA TYR A 1203 −11.655 7.548 −12.870 1.00 1.00 H ATOM 3627 HB2 TYR A 1203 −13.602 7.001 −10.516 1.00 1.00 H ATOM 3628 HB1 TYR A 1203 −14.110 7.472 −12.193 1.00 1.00 H ATOM 3629 HD2 TYR A 1203 −11.845 8.575 −9.348 1.00 1.00 H ATOM 3630 HE2 TYR A 1203 −11.419 10.924 −8.778 1.00 1.00 H ATOM 3631 HE1 TYR A 1203 −13.707 12.091 −12.169 1.00 1.00 H ATOM 3632 HD1 TYR A 1203 −14.055 9.777 −12.791 1.00 1.00 H ATOM 3633 HH TYR A 1203 −11.882 13.224 −9.357 1.00 1.00 H ATOM 3634 HN TYR A 1203 −12.352 4.739 −12.277 1.00 1.00 H ATOM 3635 N MET A 1204 −9.630 6.730 −11.455 1.00 1.00 N ATOM 3636 CA MET A 1204 −8.511 6.426 −10.540 1.00 1.00 C ATOM 3637 C MET A 1204 −8.577 4.947 −10.144 1.00 1.00 C ATOM 3638 O MET A 1204 −8.605 4.109 −11.037 1.00 1.00 O ATOM 3639 CB MET A 1204 −8.503 7.545 −9.414 1.00 1.00 C ATOM 3640 CG MET A 1204 −8.273 8.984 −10.029 1.00 1.00 C ATOM 3641 SD MET A 1204 −6.694 9.115 −10.854 1.00 1.00 S ATOM 3642 CE MET A 1204 −6.780 10.947 −11.186 1.00 1.00 C ATOM 3643 HA MET A 1204 −7.551 6.521 −11.013 1.00 1.00 H ATOM 3644 HB1 MET A 1204 −9.432 7.634 −8.938 1.00 1.00 H ATOM 3645 HB2 MET A 1204 −7.736 7.358 −8.605 1.00 1.00 H ATOM 3646 HG1 MET A 1204 −8.322 9.751 −9.231 1.00 1.00 H ATOM 3647 HG2 MET A 1204 −9.152 9.231 −10.665 1.00 1.00 H ATOM 3648 HE1 MET A 1204 −5.895 11.190 −11.714 1.00 1.00 H ATOM 3649 HE2 MET A 1204 −6.821 11.404 −10.174 1.00 1.00 H ATOM 3650 HE3 MET A 1204 −7.635 11.213 −11.826 1.00 1.00 H ATOM 3651 HN MET A 1204 −9.362 6.961 −12.390 1.00 1.00 H ATOM 3652 N ASP A 1205 −8.570 4.530 −8.825 1.00 1.00 N ATOM 3653 CA ASP A 1205 −8.641 3.078 −8.525 1.00 1.00 C ATOM 3654 C ASP A 1205 −10.081 2.743 −8.380 1.00 1.00 C ATOM 3655 O ASP A 1205 −10.472 2.137 −7.391 1.00 1.00 O ATOM 3656 CB ASP A 1205 −7.845 2.657 −7.262 1.00 1.00 C ATOM 3657 CG ASP A 1205 −8.498 2.915 −5.861 1.00 1.00 C ATOM 3658 OD1 ASP A 1205 −9.420 3.771 −5.877 1.00 1.00 O ATOM 3659 OD2 ASP A 1205 −8.132 2.302 −4.788 1.00 1.00 O ATOM 3660 HA ASP A 1205 −8.217 2.539 −9.391 1.00 1.00 H ATOM 3661 HB1 ASP A 1205 −6.868 3.189 −7.285 1.00 1.00 H ATOM 3662 HB2 ASP A 1205 −7.722 1.577 −7.352 1.00 1.00 H ATOM 3663 HN ASP A 1205 −8.641 5.187 −8.116 1.00 1.00 H ATOM 3664 N ASP A 1206 −10.983 3.146 −9.280 1.00 1.00 N ATOM 3665 CA ASP A 1206 −12.423 2.887 −9.079 1.00 1.00 C ATOM 3666 C ASP A 1206 −13.199 2.657 −10.343 1.00 1.00 C ATOM 3667 O ASP A 1206 −13.264 3.418 −11.290 1.00 1.00 O ATOM 3668 CB ASP A 1206 −13.051 4.057 −8.321 1.00 1.00 C ATOM 3669 CG ASP A 1206 −12.194 4.197 −7.110 1.00 1.00 C ATOM 3670 OD1 ASP A 1206 −11.165 4.853 −7.023 1.00 1.00 O ATOM 3671 OD2 ASP A 1206 −12.455 3.693 −6.027 1.00 1.00 O ATOM 3672 HA ASP A 1206 −12.539 1.984 −8.437 1.00 1.00 H ATOM 3673 HB1 ASP A 1206 −14.075 3.751 −7.970 1.00 1.00 H ATOM 3674 HB2 ASP A 1206 −13.083 5.065 −8.754 1.00 1.00 H ATOM 3675 HN ASP A 1206 −10.793 3.745 −10.075 1.00 1.00 H ATOM 3676 N VAL A 1207 −13.866 1.461 −10.432 1.00 1.00 N ATOM 3677 CA VAL A 1207 −14.365 1.071 −11.762 1.00 1.00 C ATOM 3678 C VAL A 1207 −15.709 0.400 −11.785 1.00 1.00 C ATOM 3679 O VAL A 1207 −16.231 0.032 −10.743 1.00 1.00 O ATOM 3680 CB VAL A 1207 −13.272 0.196 −12.460 1.00 1.00 C ATOM 3681 CG1 VAL A 1207 −11.852 0.794 −12.522 1.00 1.00 C ATOM 3682 CG2 VAL A 1207 −13.222 −1.198 −11.764 1.00 1.00 C ATOM 3683 HA VAL A 1207 −14.484 1.969 −12.402 1.00 1.00 H ATOM 3684 HB VAL A 1207 −13.630 −0.073 −13.461 1.00 1.00 H ATOM 3685 HG11 VAL A 1207 −11.109 0.164 −13.129 1.00 1.00 H ATOM 3686 HG12 VAL A 1207 −11.877 1.785 −12.970 1.00 1.00 H ATOM 3687 HG13 VAL A 1207 −11.441 0.836 −11.503 1.00 1.00 H ATOM 3688 HG21 VAL A 1207 −14.181 −1.722 −11.773 1.00 1.00 H ATOM 3689 HG22 VAL A 1207 −12.480 −1.869 −12.206 1.00 1.00 H ATOM 3690 HG23 VAL A 1207 −12.965 −1.003 −10.741 1.00 1.00 H ATOM 3691 HN VAL A 1207 −13.953 0.772 −9.706 1.00 1.00 H ATOM 3692 N VAL A 1208 −16.172 0.324 −13.032 1.00 1.00 N ATOM 3693 CA VAL A 1208 −17.507 −0.241 −13.314 1.00 1.00 C ATOM 3694 C VAL A 1208 −17.316 −1.114 −14.525 1.00 1.00 C ATOM 3695 O VAL A 1208 −17.475 −0.571 −15.619 1.00 1.00 O ATOM 3696 CB VAL A 1208 −18.550 0.858 −13.611 1.00 1.00 C ATOM 3697 CG1 VAL A 1208 −19.951 0.316 −13.959 1.00 1.00 C ATOM 3698 CG2 VAL A 1208 −18.524 1.820 −12.364 1.00 1.00 C ATOM 3699 HA VAL A 1208 −17.900 −0.832 −12.542 1.00 1.00 H ATOM 3700 HB VAL A 1208 −18.320 1.547 −14.427 1.00 1.00 H ATOM 3701 HG11 VAL A 1208 −19.862 −0.484 −14.674 1.00 1.00 H ATOM 3702 HG12 VAL A 1208 −20.522 −0.035 −13.092 1.00 1.00 H ATOM 3703 HG13 VAL A 1208 −20.560 1.055 −14.457 1.00 1.00 H ATOM 3704 HG21 VAL A 1208 −17.590 2.346 −12.267 1.00 1.00 H ATOM 3705 HG22 VAL A 1208 −19.334 2.594 −12.407 1.00 1.00 H ATOM 3706 HG23 VAL A 1208 −18.593 1.155 −11.453 1.00 1.00 H ATOM 3707 HN VAL A 1208 −15.747 0.776 −13.830 1.00 1.00 H ATOM 3708 N LEU A 1209 −16.991 −2.445 −14.390 1.00 1.00 N ATOM 3709 CA LEU A 1209 −16.640 −3.307 −15.539 1.00 1.00 C ATOM 3710 C LEU A 1209 −17.734 −4.275 −15.780 1.00 1.00 C ATOM 3711 O LEU A 1209 −17.509 −5.470 −15.799 1.00 1.00 O ATOM 3712 CB LEU A 1209 −15.315 −4.011 −15.135 1.00 1.00 C ATOM 3713 CG LEU A 1209 −14.113 −3.105 −14.851 1.00 1.00 C ATOM 3714 CD1 LEU A 1209 −12.900 −4.006 −14.431 1.00 1.00 C ATOM 3715 CD2 LEU A 1209 −13.720 −2.278 −16.078 1.00 1.00 C ATOM 3716 HA LEU A 1209 −16.504 −2.784 −16.531 1.00 1.00 H ATOM 3717 HB1 LEU A 1209 −15.105 −4.733 −15.919 1.00 1.00 H ATOM 3718 HB2 LEU A 1209 −15.465 −4.561 −14.236 1.00 1.00 H ATOM 3719 HG LEU A 1209 −14.339 −2.417 −14.005 1.00 1.00 H ATOM 3720 HD21 LEU A 1209 −13.557 −2.816 −17.031 1.00 1.00 H ATOM 3721 HD22 LEU A 1209 −14.448 −1.525 −16.362 1.00 1.00 H ATOM 3722 HD23 LEU A 1209 −12.788 −1.701 −15.879 1.00 1.00 H ATOM 3723 HD11 LEU A 1209 −12.662 −4.766 −15.181 1.00 1.00 H ATOM 3724 HD12 LEU A 1209 −11.972 −3.436 −14.209 1.00 1.00 H ATOM 3725 HD13 LEU A 1209 −13.079 −4.665 −13.584 1.00 1.00 H ATOM 3726 HN LEU A 1209 −16.954 −2.849 −13.492 1.00 1.00 H ATOM 3727 N GLY A 1210 −18.963 −3.841 −15.957 1.00 1.00 N ATOM 3728 CA GLY A 1210 −20.053 −4.801 −16.265 1.00 1.00 C ATOM 3729 C GLY A 1210 −20.285 −5.112 −17.679 1.00 1.00 C ATOM 3730 O GLY A 1210 −21.136 −5.920 −17.933 1.00 1.00 O ATOM 3731 HA2 GLY A 1210 −21.012 −4.420 −15.929 1.00 1.00 H ATOM 3732 HA1 GLY A 1210 −19.883 −5.754 −15.749 1.00 1.00 H ATOM 3733 HN GLY A 1210 −19.128 −2.869 −15.942 1.00 1.00 H ATOM 3734 N ALA A 1211 −19.653 −4.494 −18.702 1.00 1.00 N ATOM 3735 CA ALA A 1211 −20.062 −4.863 −20.069 1.00 1.00 C ATOM 3736 C ALA A 1211 −21.578 −4.877 −20.270 1.00 1.00 C ATOM 3737 O ALA A 1211 −22.166 −5.758 −20.873 1.00 1.00 O ATOM 3738 CB ALA A 1211 −19.367 −6.218 −20.343 1.00 1.00 C ATOM 3739 HA ALA A 1211 −19.618 −4.188 −20.795 1.00 1.00 H ATOM 3740 HB1 ALA A 1211 −18.289 −5.957 −20.421 1.00 1.00 H ATOM 3741 HB2 ALA A 1211 −19.420 −6.961 −19.516 1.00 1.00 H ATOM 3742 HB3 ALA A 1211 −19.713 −6.636 −21.317 1.00 1.00 H ATOM 3743 HN ALA A 1211 −18.834 −3.990 −18.531 1.00 1.00 H ATOM 3744 N LYS A 1212 −22.253 −3.854 −19.666 1.00 1.00 N ATOM 3745 CA LYS A 1212 −23.693 −3.848 −19.504 1.00 1.00 C ATOM 3746 C LYS A 1212 −24.475 −4.295 −20.710 1.00 1.00 C ATOM 3747 O LYS A 1212 −23.948 −4.321 −21.778 1.00 1.00 O ATOM 3748 CB LYS A 1212 −24.099 −2.401 −18.997 1.00 1.00 C ATOM 3749 CG LYS A 1212 −25.590 −2.293 −18.556 1.00 1.00 C ATOM 3750 CD LYS A 1212 −25.799 −0.919 −17.875 1.00 1.00 C ATOM 3751 CE LYS A 1212 −27.250 −0.739 −17.362 1.00 1.00 C ATOM 3752 NZ LYS A 1212 −27.495 0.481 −16.549 1.00 1.00 N ATOM 3753 HA LYS A 1212 −24.016 −4.490 −18.662 1.00 1.00 H ATOM 3754 HB1 LYS A 1212 −23.844 −1.686 −19.808 1.00 1.00 H ATOM 3755 HB2 LYS A 1212 −23.509 −2.195 −18.148 1.00 1.00 H ATOM 3756 HG1 LYS A 1212 −25.837 −3.132 −17.908 1.00 1.00 H ATOM 3757 HG2 LYS A 1212 −26.164 −2.389 −19.491 1.00 1.00 H ATOM 3758 HD1 LYS A 1212 −25.572 −0.160 −18.607 1.00 1.00 H ATOM 3759 HD2 LYS A 1212 −25.082 −0.865 −17.024 1.00 1.00 H ATOM 3760 HE1 LYS A 1212 −28.032 −0.812 −18.143 1.00 1.00 H ATOM 3761 HE2 LYS A 1212 −27.372 −1.571 −16.654 1.00 1.00 H ATOM 3762 HZ1 LYS A 1212 −27.653 1.379 −17.161 1.00 1.00 H ATOM 3763 HZ2 LYS A 1212 −28.325 0.486 −15.918 1.00 1.00 H ATOM 3764 HZ3 LYS A 1212 −26.701 0.653 −15.839 1.00 1.00 H ATOM 3765 HN LYS A 1212 −21.738 −3.170 −19.235 1.00 1.00 H ATOM 3766 N SER A 1213 −25.760 −4.646 −20.542 1.00 1.00 N ATOM 3767 CA SER A 1213 −26.758 −4.542 −21.599 1.00 1.00 C ATOM 3768 C SER A 1213 −28.117 −5.132 −21.207 1.00 1.00 C ATOM 3769 O SER A 1213 −29.132 −4.471 −21.330 1.00 1.00 O ATOM 3770 CB SER A 1213 −26.285 −5.090 −22.979 1.00 1.00 C ATOM 3771 OG SER A 1213 −25.685 −6.412 −22.983 1.00 1.00 O ATOM 3772 HA SER A 1213 −26.992 −3.457 −21.743 1.00 1.00 H ATOM 3773 HB1 SER A 1213 −25.638 −4.414 −23.503 1.00 1.00 H ATOM 3774 HB2 SER A 1213 −27.190 −5.213 −23.614 1.00 1.00 H ATOM 3775 HG SER A 1213 −26.282 −7.094 −22.733 1.00 1.00 H ATOM 3776 HN SER A 1213 −26.039 −4.762 −19.598 1.00 1.00 H ATOM 3777 N VAL A 1214 −28.138 −6.422 −20.693 1.00 1.00 N ATOM 3778 CA VAL A 1214 −29.348 −7.114 −20.236 1.00 1.00 C ATOM 3779 C VAL A 1214 −29.099 −7.666 −18.837 1.00 1.00 C ATOM 3780 O VAL A 1214 −29.582 −8.767 −18.502 1.00 1.00 O ATOM 3781 CB VAL A 1214 −29.977 −8.078 −21.286 1.00 1.00 C ATOM 3782 CG1 VAL A 1214 −30.404 −7.295 −22.561 1.00 1.00 C ATOM 3783 CG2 VAL A 1214 −29.089 −9.323 −21.686 1.00 1.00 C ATOM 3784 HA VAL A 1214 −30.029 −6.265 −20.078 1.00 1.00 H ATOM 3785 HB VAL A 1214 −30.958 −8.361 −20.870 1.00 1.00 H ATOM 3786 HG11 VAL A 1214 −31.015 −6.361 −22.344 1.00 1.00 H ATOM 3787 HG12 VAL A 1214 −30.968 −7.871 −23.263 1.00 1.00 H ATOM 3788 HG13 VAL A 1214 −29.534 −7.056 −23.133 1.00 1.00 H ATOM 3789 HG21 VAL A 1214 −29.061 −9.958 −20.740 1.00 1.00 H ATOM 3790 HG22 VAL A 1214 −29.650 −9.892 −22.471 1.00 1.00 H ATOM 3791 HG23 VAL A 1214 −28.086 −9.095 −22.002 1.00 1.00 H ATOM 3792 HN VAL A 1214 −27.302 −6.978 −20.631 1.00 1.00 H ATOM 3793 N GLN A 1215 −28.334 −6.932 −18.006 1.00 1.00 N ATOM 3794 CA GLN A 1215 −28.095 −7.350 −16.605 1.00 1.00 C ATOM 3795 C GLN A 1215 −27.475 −8.673 −16.479 1.00 1.00 C ATOM 3796 O GLN A 1215 −27.659 −9.484 −15.553 1.00 1.00 O ATOM 3797 CB GLN A 1215 −29.330 −7.103 −15.751 1.00 1.00 C ATOM 3798 CG GLN A 1215 −30.040 −5.767 −16.129 1.00 1.00 C ATOM 3799 CD GLN A 1215 −29.052 −4.597 −15.892 1.00 1.00 C ATOM 3800 OE1 GLN A 1215 −28.748 −3.951 −16.885 1.00 1.00 O ATOM 3801 NE2 GLN A 1215 −28.533 −4.325 −14.682 1.00 1.00 N ATOM 3802 HA GLN A 1215 −27.396 −6.606 −16.194 1.00 1.00 H ATOM 3803 HB1 GLN A 1215 −30.009 −7.942 −15.880 1.00 1.00 H ATOM 3804 HB2 GLN A 1215 −28.981 −7.198 −14.723 1.00 1.00 H ATOM 3805 HG1 GLN A 1215 −30.356 −5.876 −17.149 1.00 1.00 H ATOM 3806 HG2 GLN A 1215 −30.931 −5.621 −15.551 1.00 1.00 H ATOM 3807 HE22 GLN A 1215 −27.880 −3.532 −14.502 1.00 1.00 H ATOM 3808 HE21 GLN A 1215 −28.685 −4.887 −13.896 1.00 1.00 H ATOM 3809 HN GLN A 1215 −28.033 −6.014 −18.250 1.00 1.00 H ATOM 3810 N HIS A 1216 −26.588 −8.995 −17.481 1.00 1.00 N ATOM 3811 CA HIS A 1216 −25.737 −10.201 −17.388 1.00 1.00 C ATOM 3812 C HIS A 1216 −24.581 −9.832 −16.510 1.00 1.00 C ATOM 3813 O HIS A 1216 −23.486 −9.902 −16.989 1.00 1.00 O ATOM 3814 CB HIS A 1216 −25.329 −10.656 −18.763 1.00 1.00 C ATOM 3815 CG HIS A 1216 −24.448 −9.722 −19.575 1.00 1.00 C ATOM 3816 ND1 HIS A 1216 −23.173 −9.551 −19.425 1.00 1.00 N ATOM 3817 CD2 HIS A 1216 −24.818 −9.026 −20.647 1.00 1.00 C ATOM 3818 CE1 HIS A 1216 −22.687 −8.768 −20.366 1.00 1.00 C ATOM 3819 NE2 HIS A 1216 −23.630 −8.405 −21.093 1.00 1.00 N ATOM 3820 HA HIS A 1216 −26.290 −10.946 −16.881 1.00 1.00 H ATOM 3821 HB1 HIS A 1216 −24.812 −11.587 −18.725 1.00 1.00 H ATOM 3822 HB2 HIS A 1216 −26.230 −10.778 −19.373 1.00 1.00 H ATOM 3823 HD2 HIS A 1216 −25.848 −9.063 −21.040 1.00 1.00 H ATOM 3824 HE1 HIS A 1216 −21.626 −8.484 −20.515 1.00 1.00 H ATOM 3825 HD1 HIS A 1216 −22.592 −10.002 −18.689 1.00 1.00 H ATOM 3826 HN HIS A 1216 −26.475 −8.428 −18.268 1.00 1.00 H ATOM 3827 N LEU A 1217 −24.787 −9.449 −15.198 1.00 1.00 N ATOM 3828 CA LEU A 1217 −23.637 −9.198 −14.266 1.00 1.00 C ATOM 3829 C LEU A 1217 −23.354 −10.363 −13.307 1.00 1.00 C ATOM 3830 O LEU A 1217 −22.953 −10.115 −12.162 1.00 1.00 O ATOM 3831 CB LEU A 1217 −23.924 −7.958 −13.403 1.00 1.00 C ATOM 3832 CG LEU A 1217 −24.353 −6.615 −14.107 1.00 1.00 C ATOM 3833 CD1 LEU A 1217 −24.753 −5.609 −13.046 1.00 1.00 C ATOM 3834 CD2 LEU A 1217 −23.200 −5.970 −14.947 1.00 1.00 C ATOM 3835 HA LEU A 1217 −22.666 −8.943 −14.723 1.00 1.00 H ATOM 3836 HB1 LEU A 1217 −24.770 −8.242 −12.782 1.00 1.00 H ATOM 3837 HB2 LEU A 1217 −23.114 −7.761 −12.720 1.00 1.00 H ATOM 3838 HG LEU A 1217 −25.213 −6.801 −14.735 1.00 1.00 H ATOM 3839 HD21 LEU A 1217 −23.366 −5.005 −15.369 1.00 1.00 H ATOM 3840 HD22 LEU A 1217 −22.318 −5.934 −14.303 1.00 1.00 H ATOM 3841 HD23 LEU A 1217 −22.848 −6.625 −15.769 1.00 1.00 H ATOM 3842 HD11 LEU A 1217 −25.544 −6.060 −12.383 1.00 1.00 H ATOM 3843 HD12 LEU A 1217 −25.233 −4.807 −13.542 1.00 1.00 H ATOM 3844 HD13 LEU A 1217 −23.872 −5.241 −12.481 1.00 1.00 H ATOM 3845 HN LEU A 1217 −25.693 −9.497 −14.786 1.00 1.00 H ATOM 3846 N GLU A 1218 −23.489 −11.657 −13.712 1.00 1.00 N ATOM 3847 CA GLU A 1218 −23.146 −12.732 −12.813 1.00 1.00 C ATOM 3848 C GLU A 1218 −22.028 −13.555 −13.354 1.00 1.00 C ATOM 3849 O GLU A 1218 −20.952 −13.535 −12.780 1.00 1.00 O ATOM 3850 CB GLU A 1218 −24.499 −13.489 −12.546 1.00 1.00 C ATOM 3851 CG GLU A 1218 −25.753 −12.609 −12.336 1.00 1.00 C ATOM 3852 CD GLU A 1218 −25.551 −11.591 −11.209 1.00 1.00 C ATOM 3853 OE1 GLU A 1218 −24.994 −11.946 −10.125 1.00 1.00 O ATOM 3854 OE2 GLU A 1218 −25.906 −10.409 −11.334 1.00 1.00 O ATOM 3855 HA GLU A 1218 −22.826 −12.428 −11.809 1.00 1.00 H ATOM 3856 HB1 GLU A 1218 −24.545 −14.139 −11.599 1.00 1.00 H ATOM 3857 HB2 GLU A 1218 −24.725 −14.057 −13.463 1.00 1.00 H ATOM 3858 HG1 GLU A 1218 −25.993 −12.040 −13.224 1.00 1.00 H ATOM 3859 HG2 GLU A 1218 −26.581 −13.255 −12.049 1.00 1.00 H ATOM 3860 HN GLU A 1218 −23.733 −11.868 −14.684 1.00 1.00 H ATOM 3861 N SER A 1219 −22.100 −14.320 −14.483 1.00 1.00 N ATOM 3862 CA SER A 1219 −20.900 −14.972 −14.987 1.00 1.00 C ATOM 3863 C SER A 1219 −19.811 −14.081 −15.539 1.00 1.00 C ATOM 3864 O SER A 1219 −18.609 −14.187 −15.170 1.00 1.00 O ATOM 3865 CB SER A 1219 −21.329 −16.010 −16.035 1.00 1.00 C ATOM 3866 OG SER A 1219 −22.463 −16.737 −15.444 1.00 1.00 O ATOM 3867 HA SER A 1219 −20.481 −15.549 −14.119 1.00 1.00 H ATOM 3868 HB1 SER A 1219 −21.622 −15.509 −16.947 1.00 1.00 H ATOM 3869 HB2 SER A 1219 −20.489 −16.677 −16.342 1.00 1.00 H ATOM 3870 HG SER A 1219 −22.276 −17.238 −14.654 1.00 1.00 H ATOM 3871 HN SER A 1219 −22.982 −14.448 −14.969 1.00 1.00 H ATOM 3872 N LEU A 1220 −20.074 −13.127 −16.512 1.00 1.00 N ATOM 3873 CA LEU A 1220 −18.939 −12.311 −16.939 1.00 1.00 C ATOM 3874 C LEU A 1220 −18.426 −11.491 −15.734 1.00 1.00 C ATOM 3875 O LEU A 1220 −17.266 −11.198 −15.723 1.00 1.00 O ATOM 3876 CB LEU A 1220 −19.398 −11.398 −18.121 1.00 1.00 C ATOM 3877 CG LEU A 1220 −18.351 −10.300 −18.524 1.00 1.00 C ATOM 3878 CD1 LEU A 1220 −18.444 −10.003 −20.054 1.00 1.00 C ATOM 3879 CD2 LEU A 1220 −18.606 −8.970 −17.785 1.00 1.00 C ATOM 3880 HA LEU A 1220 −18.203 −13.035 −17.343 1.00 1.00 H ATOM 3881 HB1 LEU A 1220 −19.700 −12.053 −19.000 1.00 1.00 H ATOM 3882 HB2 LEU A 1220 −20.281 −10.948 −17.770 1.00 1.00 H ATOM 3883 HG LEU A 1220 −17.302 −10.647 −18.423 1.00 1.00 H ATOM 3884 HD21 LEU A 1220 −18.526 −9.100 −16.688 1.00 1.00 H ATOM 3885 HD22 LEU A 1220 −17.894 −8.160 −18.123 1.00 1.00 H ATOM 3886 HD23 LEU A 1220 −19.604 −8.663 −18.073 1.00 1.00 H ATOM 3887 HD11 LEU A 1220 −17.945 −9.047 −20.219 1.00 1.00 H ATOM 3888 HD12 LEU A 1220 −19.479 −9.952 −20.306 1.00 1.00 H ATOM 3889 HD13 LEU A 1220 −17.924 −10.744 −20.672 1.00 1.00 H ATOM 3890 HN LEU A 1220 −21.058 −12.965 −16.744 1.00 1.00 H ATOM 3891 N PHE A 1221 −19.270 −11.235 −14.657 1.00 1.00 N ATOM 3892 CA PHE A 1221 −18.778 −10.634 −13.379 1.00 1.00 C ATOM 3893 C PHE A 1221 −17.855 −11.596 −12.738 1.00 1.00 C ATOM 3894 O PHE A 1221 −16.751 −11.192 −12.452 1.00 1.00 O ATOM 3895 CB PHE A 1221 −19.920 −10.146 −12.476 1.00 1.00 C ATOM 3896 CG PHE A 1221 −19.390 −9.634 −11.133 1.00 1.00 C ATOM 3897 CD1 PHE A 1221 −19.222 −8.266 −11.036 1.00 1.00 C ATOM 3898 CD2 PHE A 1221 −19.073 −10.500 −10.085 1.00 1.00 C ATOM 3899 CE1 PHE A 1221 −18.781 −7.722 −9.842 1.00 1.00 C ATOM 3900 CE2 PHE A 1221 −18.608 −9.951 −8.874 1.00 1.00 C ATOM 3901 CZ PHE A 1221 −18.580 −8.560 −8.721 1.00 1.00 C ATOM 3902 HA PHE A 1221 −18.194 −9.713 −13.649 1.00 1.00 H ATOM 3903 HB1 PHE A 1221 −20.483 −9.361 −13.033 1.00 1.00 H ATOM 3904 HB2 PHE A 1221 −20.676 −10.986 −12.402 1.00 1.00 H ATOM 3905 HD2 PHE A 1221 −19.248 −11.561 −10.206 1.00 1.00 H ATOM 3906 HE2 PHE A 1221 −18.348 −10.618 −8.056 1.00 1.00 H ATOM 3907 HZ PHE A 1221 −18.294 −8.123 −7.779 1.00 1.00 H ATOM 3908 HE1 PHE A 1221 −18.535 −6.712 −9.833 1.00 1.00 H ATOM 3909 HD1 PHE A 1221 −19.384 −7.634 −11.910 1.00 1.00 H ATOM 3910 HN PHE A 1221 −20.214 −11.510 −14.690 1.00 1.00 H ATOM 3911 N THR A 1222 −18.267 −12.857 −12.484 1.00 1.00 N ATOM 3912 CA THR A 1222 −17.281 −13.748 −11.810 1.00 1.00 C ATOM 3913 C THR A 1222 −16.012 −13.976 −12.640 1.00 1.00 C ATOM 3914 O THR A 1222 −14.905 −13.925 −12.125 1.00 1.00 O ATOM 3915 CB THR A 1222 −17.847 −15.173 −11.466 1.00 1.00 C ATOM 3916 OG1 THR A 1222 −18.255 −15.763 −12.727 1.00 1.00 O ATOM 3917 CG2 THR A 1222 −18.974 −15.144 −10.383 1.00 1.00 C ATOM 3918 HA THR A 1222 −16.955 −13.243 −10.872 1.00 1.00 H ATOM 3919 HB THR A 1222 −16.969 −15.740 −11.054 1.00 1.00 H ATOM 3920 HG1 THR A 1222 −18.704 −16.578 −12.544 1.00 1.00 H ATOM 3921 HG23 THR A 1222 −19.757 −14.478 −10.788 1.00 1.00 H ATOM 3922 HG21 THR A 1222 −19.309 −16.160 −10.175 1.00 1.00 H ATOM 3923 HG22 THR A 1222 −18.629 −14.760 −9.423 1.00 1.00 H ATOM 3924 HN THR A 1222 −19.183 −13.138 −12.734 1.00 1.00 H ATOM 3925 N ALA A 1223 −16.122 −14.273 −13.960 1.00 1.00 N ATOM 3926 CA ALA A 1223 −14.952 −14.330 −14.822 1.00 1.00 C ATOM 3927 C ALA A 1223 −14.101 −13.046 −14.815 1.00 1.00 C ATOM 3928 O ALA A 1223 −12.916 −13.181 −14.596 1.00 1.00 O ATOM 3929 CB ALA A 1223 −15.294 −14.755 −16.299 1.00 1.00 C ATOM 3930 HA ALA A 1223 −14.314 −15.152 −14.419 1.00 1.00 H ATOM 3931 HB1 ALA A 1223 −14.456 −14.843 −16.962 1.00 1.00 H ATOM 3932 HB2 ALA A 1223 −15.769 −15.760 −16.224 1.00 1.00 H ATOM 3933 HB3 ALA A 1223 −16.017 −14.046 −16.663 1.00 1.00 H ATOM 3934 HN ALA A 1223 −17.062 −14.375 −14.326 1.00 1.00 H ATOM 3935 N VAL A 1224 −14.611 −11.803 −14.951 1.00 1.00 N ATOM 3936 CA VAL A 1224 −13.850 −10.591 −14.707 1.00 1.00 C ATOM 3937 C VAL A 1224 −13.231 −10.392 −13.336 1.00 1.00 C ATOM 3938 O VAL A 1224 −12.035 −10.187 −13.246 1.00 1.00 O ATOM 3939 CB VAL A 1224 −14.717 −9.292 −14.844 1.00 1.00 C ATOM 3940 CG1 VAL A 1224 −14.085 −7.975 −14.193 1.00 1.00 C ATOM 3941 CG2 VAL A 1224 −15.010 −9.052 −16.361 1.00 1.00 C ATOM 3942 HA VAL A 1224 −13.043 −10.492 −15.483 1.00 1.00 H ATOM 3943 HB VAL A 1224 −15.631 −9.413 −14.246 1.00 1.00 H ATOM 3944 HG11 VAL A 1224 −13.020 −7.884 −14.572 1.00 1.00 H ATOM 3945 HG12 VAL A 1224 −14.598 −7.047 −14.490 1.00 1.00 H ATOM 3946 HG13 VAL A 1224 −14.088 −8.057 −13.121 1.00 1.00 H ATOM 3947 HG21 VAL A 1224 −15.486 −9.915 −16.872 1.00 1.00 H ATOM 3948 HG22 VAL A 1224 −15.681 −8.183 −16.541 1.00 1.00 H ATOM 3949 HG23 VAL A 1224 −14.088 −8.801 −16.900 1.00 1.00 H ATOM 3950 HN VAL A 1224 −15.609 −11.708 −15.051 1.00 1.00 H ATOM 3951 N THR A 1225 −14.023 −10.547 −12.271 1.00 1.00 N ATOM 3952 CA THR A 1225 −13.399 −10.380 −10.975 1.00 1.00 C ATOM 3953 C THR A 1225 −12.441 −11.528 −10.734 1.00 1.00 C ATOM 3954 O THR A 1225 −11.496 −11.381 −10.016 1.00 1.00 O ATOM 3955 CB THR A 1225 −14.356 −10.275 −9.760 1.00 1.00 C ATOM 3956 OG1 THR A 1225 −15.044 −11.501 −9.799 1.00 1.00 O ATOM 3957 CG2 THR A 1225 −15.310 −9.102 −9.837 1.00 1.00 C ATOM 3958 HA THR A 1225 −12.768 −9.462 −10.914 1.00 1.00 H ATOM 3959 HB THR A 1225 −13.754 −10.293 −8.834 1.00 1.00 H ATOM 3960 HG1 THR A 1225 −15.640 −11.737 −9.093 1.00 1.00 H ATOM 3961 HG23 THR A 1225 −15.982 −8.949 −9.017 1.00 1.00 H ATOM 3962 HG21 THR A 1225 −15.953 −9.185 −10.746 1.00 1.00 H ATOM 3963 HG22 THR A 1225 −14.668 −8.182 −9.900 1.00 1.00 H ATOM 3964 HN THR A 1225 −15.038 −10.731 −12.344 1.00 1.00 H ATOM 3965 N ASN A 1226 −12.672 −12.758 −11.202 1.00 1.00 N ATOM 3966 CA ASN A 1226 −11.762 −13.886 −10.988 1.00 1.00 C ATOM 3967 C ASN A 1226 −10.427 −13.661 −11.739 1.00 1.00 C ATOM 3968 O ASN A 1226 −9.354 −13.909 −11.184 1.00 1.00 O ATOM 3969 CB ASN A 1226 −12.259 −15.227 −11.522 1.00 1.00 C ATOM 3970 CG ASN A 1226 −11.211 −16.351 −11.297 1.00 1.00 C ATOM 3971 OD1 ASN A 1226 −11.372 −17.070 −10.316 1.00 1.00 O ATOM 3972 ND2 ASN A 1226 −10.156 −16.522 −12.127 1.00 1.00 N ATOM 3973 HA ASN A 1226 −11.601 −13.928 −9.870 1.00 1.00 H ATOM 3974 HB1 ASN A 1226 −13.151 −15.559 −10.906 1.00 1.00 H ATOM 3975 HB2 ASN A 1226 −12.605 −15.184 −12.598 1.00 1.00 H ATOM 3976 HD22 ASN A 1226 −9.498 −17.241 −11.874 1.00 1.00 H ATOM 3977 HD21 ASN A 1226 −10.003 −16.038 −12.998 1.00 1.00 H ATOM 3978 HN ASN A 1226 −13.480 −12.910 −11.739 1.00 1.00 H ATOM 3979 N PHE A 1227 −10.547 −13.219 −13.008 1.00 1.00 N ATOM 3980 CA PHE A 1227 −9.334 −12.847 −13.684 1.00 1.00 C ATOM 3981 C PHE A 1227 −8.675 −11.733 −12.940 1.00 1.00 C ATOM 3982 O PHE A 1227 −7.463 −11.769 −12.795 1.00 1.00 O ATOM 3983 CB PHE A 1227 −9.610 −12.371 −15.127 1.00 1.00 C ATOM 3984 CG PHE A 1227 −10.001 −13.479 −16.131 1.00 1.00 C ATOM 3985 CD1 PHE A 1227 −11.167 −13.420 −16.917 1.00 1.00 C ATOM 3986 CD2 PHE A 1227 −9.074 −14.537 −16.313 1.00 1.00 C ATOM 3987 CE1 PHE A 1227 −11.490 −14.422 −17.810 1.00 1.00 C ATOM 3988 CE2 PHE A 1227 −9.387 −15.568 −17.182 1.00 1.00 C ATOM 3989 CZ PHE A 1227 −10.603 −15.486 −17.890 1.00 1.00 C ATOM 3990 HA PHE A 1227 −8.583 −13.688 −13.678 1.00 1.00 H ATOM 3991 HB1 PHE A 1227 −10.341 −11.531 −15.156 1.00 1.00 H ATOM 3992 HB2 PHE A 1227 −8.653 −11.958 −15.518 1.00 1.00 H ATOM 3993 HD2 PHE A 1227 −8.177 −14.646 −15.781 1.00 1.00 H ATOM 3994 HE2 PHE A 1227 −8.685 −16.422 −17.343 1.00 1.00 H ATOM 3995 HZ PHE A 1227 −10.864 −16.305 −18.531 1.00 1.00 H ATOM 3996 HE1 PHE A 1227 −12.381 −14.359 −18.412 1.00 1.00 H ATOM 3997 HD1 PHE A 1227 −11.880 −12.572 −16.926 1.00 1.00 H ATOM 3998 HN PHE A 1227 −11.402 −13.068 −13.460 1.00 1.00 H ATOM 3999 N LEU A 1228 −9.397 −10.699 −12.421 1.00 1.00 N ATOM 4000 CA LEU A 1228 −8.685 −9.577 −11.793 1.00 1.00 C ATOM 4001 C LEU A 1228 −8.133 −10.040 −10.463 1.00 1.00 C ATOM 4002 O LEU A 1228 −7.012 −9.649 −10.076 1.00 1.00 O ATOM 4003 CB LEU A 1228 −9.637 −8.376 −11.608 1.00 1.00 C ATOM 4004 CG LEU A 1228 −9.052 −6.975 −11.102 1.00 1.00 C ATOM 4005 CD1 LEU A 1228 −7.923 −6.403 −11.975 1.00 1.00 C ATOM 4006 CD2 LEU A 1228 −10.163 −5.891 −10.948 1.00 1.00 C ATOM 4007 HA LEU A 1228 −7.797 −9.322 −12.363 1.00 1.00 H ATOM 4008 HB1 LEU A 1228 −10.116 −8.163 −12.565 1.00 1.00 H ATOM 4009 HB2 LEU A 1228 −10.411 −8.768 −10.965 1.00 1.00 H ATOM 4010 HG LEU A 1228 −8.561 −7.152 −10.095 1.00 1.00 H ATOM 4011 HD21 LEU A 1228 −9.785 −4.923 −10.615 1.00 1.00 H ATOM 4012 HD22 LEU A 1228 −10.628 −5.798 −11.945 1.00 1.00 H ATOM 4013 HD23 LEU A 1228 −10.868 −6.311 −10.185 1.00 1.00 H ATOM 4014 HD11 LEU A 1228 −8.154 −6.274 −13.077 1.00 1.00 H ATOM 4015 HD12 LEU A 1228 −7.575 −5.403 −11.608 1.00 1.00 H ATOM 4016 HD13 LEU A 1228 −7.060 −7.052 −11.969 1.00 1.00 H ATOM 4017 HN LEU A 1228 −10.389 −10.762 −12.531 1.00 1.00 H ATOM 4018 N LEU A 1229 −8.914 −10.872 −9.740 1.00 1.00 N ATOM 4019 CA LEU A 1229 −8.524 −11.224 −8.359 1.00 1.00 C ATOM 4020 C LEU A 1229 −7.736 −12.516 −8.252 1.00 1.00 C ATOM 4021 O LEU A 1229 −6.652 −12.535 −7.666 1.00 1.00 O ATOM 4022 CB LEU A 1229 −9.837 −11.279 −7.506 1.00 1.00 C ATOM 4023 CG LEU A 1229 −9.625 −11.527 −5.966 1.00 1.00 C ATOM 4024 CD1 LEU A 1229 −10.893 −11.060 −5.203 1.00 1.00 C ATOM 4025 CD2 LEU A 1229 −9.396 −13.052 −5.649 1.00 1.00 C ATOM 4026 HA LEU A 1229 −7.933 −10.419 −7.954 1.00 1.00 H ATOM 4027 HB1 LEU A 1229 −10.271 −10.264 −7.681 1.00 1.00 H ATOM 4028 HB2 LEU A 1229 −10.547 −11.970 −7.907 1.00 1.00 H ATOM 4029 HG LEU A 1229 −8.764 −10.923 −5.633 1.00 1.00 H ATOM 4030 HD21 LEU A 1229 −8.531 −13.525 −6.111 1.00 1.00 H ATOM 4031 HD22 LEU A 1229 −9.379 −13.162 −4.567 1.00 1.00 H ATOM 4032 HD23 LEU A 1229 −10.286 −13.595 −6.018 1.00 1.00 H ATOM 4033 HD11 LEU A 1229 −10.895 −9.991 −5.090 1.00 1.00 H ATOM 4034 HD12 LEU A 1229 −11.857 −11.401 −5.626 1.00 1.00 H ATOM 4035 HD13 LEU A 1229 −10.880 −11.452 −4.169 1.00 1.00 H ATOM 4036 HN LEU A 1229 −9.797 −11.195 −10.111 1.00 1.00 H ATOM 4037 N SER A 1230 −8.252 −13.577 −8.849 1.00 1.00 N ATOM 4038 CA SER A 1230 −7.611 −14.885 −8.674 1.00 1.00 C ATOM 4039 C SER A 1230 −6.632 −15.225 −9.728 1.00 1.00 C ATOM 4040 O SER A 1230 −6.808 −16.235 −10.409 1.00 1.00 O ATOM 4041 CB SER A 1230 −8.699 −15.984 −8.499 1.00 1.00 C ATOM 4042 OG SER A 1230 −8.062 −17.163 −8.003 1.00 1.00 O ATOM 4043 HA SER A 1230 −7.033 −14.890 −7.763 1.00 1.00 H ATOM 4044 HB1 SER A 1230 −9.437 −15.563 −7.782 1.00 1.00 H ATOM 4045 HB2 SER A 1230 −9.290 −16.218 −9.389 1.00 1.00 H ATOM 4046 HG SER A 1230 −7.460 −17.562 −8.642 1.00 1.00 H ATOM 4047 HN SER A 1230 −9.059 −13.506 −9.446 1.00 1.00 H ATOM 4048 N LEU A 1231 −5.608 −14.402 −10.001 1.00 1.00 N ATOM 4049 CA LEU A 1231 −4.710 −14.705 −11.134 1.00 1.00 C ATOM 4050 C LEU A 1231 −3.267 −14.380 −10.847 1.00 1.00 C ATOM 4051 O LEU A 1231 −2.483 −15.318 −10.804 1.00 1.00 O ATOM 4052 CB LEU A 1231 −5.240 −13.890 −12.333 1.00 1.00 C ATOM 4053 CG LEU A 1231 −4.460 −13.963 −13.687 1.00 1.00 C ATOM 4054 CD1 LEU A 1231 −4.218 −15.407 −14.180 1.00 1.00 C ATOM 4055 CD2 LEU A 1231 −5.188 −13.086 −14.727 1.00 1.00 C ATOM 4056 HA LEU A 1231 −4.754 −15.767 −11.522 1.00 1.00 H ATOM 4057 HB1 LEU A 1231 −6.276 −14.171 −12.572 1.00 1.00 H ATOM 4058 HB2 LEU A 1231 −5.225 −12.849 −12.073 1.00 1.00 H ATOM 4059 HG LEU A 1231 −3.475 −13.581 −13.477 1.00 1.00 H ATOM 4060 HD21 LEU A 1231 −4.620 −12.993 −15.675 1.00 1.00 H ATOM 4061 HD22 LEU A 1231 −6.184 −13.553 −14.939 1.00 1.00 H ATOM 4062 HD23 LEU A 1231 −5.298 −12.061 −14.302 1.00 1.00 H ATOM 4063 HD11 LEU A 1231 −3.508 −15.980 −13.573 1.00 1.00 H ATOM 4064 HD12 LEU A 1231 −5.167 −15.925 −14.244 1.00 1.00 H ATOM 4065 HD13 LEU A 1231 −3.777 −15.247 −15.194 1.00 1.00 H ATOM 4066 HN LEU A 1231 −5.521 −13.533 −9.482 1.00 1.00 H ATOM 4067 N GLY A 1232 −2.921 −13.109 −10.615 1.00 1.00 N ATOM 4068 CA GLY A 1232 −1.574 −12.805 −10.153 1.00 1.00 C ATOM 4069 C GLY A 1232 −1.550 −11.704 −9.095 1.00 1.00 C ATOM 4070 O GLY A 1232 −0.517 −11.044 −9.036 1.00 1.00 O ATOM 4071 HA2 GLY A 1232 −0.952 −12.494 −11.047 1.00 1.00 H ATOM 4072 HA1 GLY A 1232 −1.076 −13.718 −9.728 1.00 1.00 H ATOM 4073 HN GLY A 1232 −3.495 −12.310 −10.758 1.00 1.00 H ATOM 4074 N ILE A 1233 −2.671 −11.564 −8.354 1.00 1.00 N ATOM 4075 CA ILE A 1233 −2.849 −10.365 −7.450 1.00 1.00 C ATOM 4076 C ILE A 1233 −3.611 −10.783 −6.194 1.00 1.00 C ATOM 4077 O ILE A 1233 −3.108 −10.539 −5.099 1.00 1.00 O ATOM 4078 CB ILE A 1233 −3.501 −9.172 −8.180 1.00 1.00 C ATOM 4079 CG1 ILE A 1233 −3.056 −8.935 −9.642 1.00 1.00 C ATOM 4080 CG2 ILE A 1233 −3.397 −7.803 −7.428 1.00 1.00 C ATOM 4081 CD1 ILE A 1233 −3.777 −7.847 −10.453 1.00 1.00 C ATOM 4082 HA ILE A 1233 −1.881 −10.031 −7.117 1.00 1.00 H ATOM 4083 HB ILE A 1233 −4.556 −9.473 −8.213 1.00 1.00 H ATOM 4084 HG11 ILE A 1233 −3.195 −9.906 −10.095 1.00 1.00 H ATOM 4085 HG12 ILE A 1233 −1.965 −8.878 −9.679 1.00 1.00 H ATOM 4086 HD11 ILE A 1233 −4.867 −7.933 −10.445 1.00 1.00 H ATOM 4087 HD12 ILE A 1233 −3.469 −6.864 −10.129 1.00 1.00 H ATOM 4088 HD13 ILE A 1233 −3.499 −7.889 −11.493 1.00 1.00 H ATOM 4089 HG21 ILE A 1233 −2.354 −7.460 −7.339 1.00 1.00 H ATOM 4090 HG22 ILE A 1233 −4.022 −7.093 −7.911 1.00 1.00 H ATOM 4091 HG23 ILE A 1233 −3.764 −7.901 −6.389 1.00 1.00 H ATOM 4092 HN ILE A 1233 −3.411 −12.245 −8.460 1.00 1.00 H ATOM 4093 N HIE A 1234 −4.822 −11.374 −6.277 1.00 1.00 N ATOM 4094 CA HIE A 1234 −5.637 −11.555 −5.111 1.00 1.00 C ATOM 4095 C HIE A 1234 −5.668 −10.251 −4.287 1.00 1.00 C ATOM 4096 O HIE A 1234 −5.074 −10.230 −3.212 1.00 1.00 O ATOM 4097 CB HIE A 1234 −4.959 −12.785 −4.406 1.00 1.00 C ATOM 4098 CG HIE A 1234 −5.411 −12.993 −3.030 1.00 1.00 C ATOM 4099 ND1 HIE A 1234 −5.027 −12.329 −1.826 1.00 1.00 N ATOM 4100 CD2 HIE A 1234 −6.259 −13.932 −2.588 1.00 1.00 C ATOM 4101 CE1 HIE A 1234 −5.537 −12.905 −0.845 1.00 1.00 C ATOM 4102 NE2 HIE A 1234 −6.309 −13.866 −1.303 1.00 1.00 N ATOM 4103 HA HIE A 1234 −6.693 −11.810 −5.350 1.00 1.00 H ATOM 4104 HB1 HIE A 1234 −5.288 −13.644 −5.035 1.00 1.00 H ATOM 4105 HB2 HIE A 1234 −3.865 −12.707 −4.468 1.00 1.00 H ATOM 4106 HD2 HIE A 1234 −6.710 −14.568 −3.301 1.00 1.00 H ATOM 4107 HE2 HIE A 1234 −6.872 −14.508 −0.693 1.00 1.00 H ATOM 4108 HE1 HIE A 1234 −5.402 −12.664 0.179 1.00 1.00 H ATOM 4109 HN HIE A 1234 −5.283 −11.512 −7.184 1.00 1.00 H ATOM 4110 N LEU A 1235 −6.327 −9.183 −4.820 1.00 1.00 N ATOM 4111 CA LEU A 1235 −6.329 −7.899 −4.125 1.00 1.00 C ATOM 4112 C LEU A 1235 −7.276 −7.878 −2.969 1.00 1.00 C ATOM 4113 O LEU A 1235 −7.875 −8.926 −2.720 1.00 1.00 O ATOM 4114 CB LEU A 1235 −6.560 −6.694 −5.027 1.00 1.00 C ATOM 4115 CG LEU A 1235 −8.030 −6.511 −5.512 1.00 1.00 C ATOM 4116 CD1 LEU A 1235 −8.080 −5.183 −6.240 1.00 1.00 C ATOM 4117 CD2 LEU A 1235 −8.669 −7.612 −6.394 1.00 1.00 C ATOM 4118 HA LEU A 1235 −5.300 −7.768 −3.692 1.00 1.00 H ATOM 4119 HB1 LEU A 1235 −6.219 −5.790 −4.540 1.00 1.00 H ATOM 4120 HB2 LEU A 1235 −5.890 −6.922 −5.893 1.00 1.00 H ATOM 4121 HG LEU A 1235 −8.702 −6.435 −4.601 1.00 1.00 H ATOM 4122 HD21 LEU A 1235 −7.979 −7.823 −7.279 1.00 1.00 H ATOM 4123 HD22 LEU A 1235 −8.934 −8.562 −5.915 1.00 1.00 H ATOM 4124 HD23 LEU A 1235 −9.606 −7.257 −6.865 1.00 1.00 H ATOM 4125 HD11 LEU A 1235 −9.121 −4.844 −6.472 1.00 1.00 H ATOM 4126 HD12 LEU A 1235 −7.545 −5.311 −7.160 1.00 1.00 H ATOM 4127 HD13 LEU A 1235 −7.684 −4.369 −5.621 1.00 1.00 H ATOM 4128 HN LEU A 1235 −6.809 −9.330 −5.635 1.00 1.00 H ATOM 4129 N ASN A 1236 −7.450 −6.753 −2.288 1.00 1.00 N ATOM 4130 CA ASN A 1236 −8.581 −6.620 −1.370 1.00 1.00 C ATOM 4131 C ASN A 1236 −9.536 −5.633 −1.963 1.00 1.00 C ATOM 4132 O ASN A 1236 −9.385 −4.439 −1.682 1.00 1.00 O ATOM 4133 CB ASN A 1236 −8.232 −5.959 0.008 1.00 1.00 C ATOM 4134 CG ASN A 1236 −7.358 −4.732 0.048 1.00 1.00 C ATOM 4135 OD1 ASN A 1236 −7.740 −3.647 0.445 1.00 1.00 O ATOM 4136 ND2 ASN A 1236 −6.074 −4.864 −0.298 1.00 1.00 N ATOM 4137 HA ASN A 1236 −9.089 −7.552 −1.084 1.00 1.00 H ATOM 4138 HB1 ASN A 1236 −9.124 −5.695 0.584 1.00 1.00 H ATOM 4139 HB2 ASN A 1236 −7.783 −6.716 0.632 1.00 1.00 H ATOM 4140 HD22 ASN A 1236 −5.600 −4.003 −0.397 1.00 1.00 H ATOM 4141 HD21 ASN A 1236 −5.607 −5.750 −0.555 1.00 1.00 H ATOM 4142 HN ASN A 1236 −6.871 −5.973 −2.419 1.00 1.00 H ATOM 4143 N PRO A 1237 −10.487 −5.925 −2.875 1.00 1.00 N ATOM 4144 CA PRO A 1237 −11.219 −4.865 −3.496 1.00 1.00 C ATOM 4145 C PRO A 1237 −12.197 −4.245 −2.517 1.00 1.00 C ATOM 4146 O PRO A 1237 −12.703 −5.027 −1.728 1.00 1.00 O ATOM 4147 CB PRO A 1237 −11.892 −5.568 −4.679 1.00 1.00 C ATOM 4148 CG PRO A 1237 −12.140 −6.955 −4.066 1.00 1.00 C ATOM 4149 CD PRO A 1237 −10.956 −7.299 −3.091 1.00 1.00 C ATOM 4150 HA PRO A 1237 −10.521 −4.089 −3.845 1.00 1.00 H ATOM 4151 HD2 PRO A 1237 −10.209 −7.909 −3.589 1.00 1.00 H ATOM 4152 HD1 PRO A 1237 −11.367 −7.825 −2.247 1.00 1.00 H ATOM 4153 HG2 PRO A 1237 −12.303 −7.728 −4.813 1.00 1.00 H ATOM 4154 HG1 PRO A 1237 −13.043 −6.834 −3.516 1.00 1.00 H ATOM 4155 HB1 PRO A 1237 −12.815 −5.110 −4.982 1.00 1.00 H ATOM 4156 HB2 PRO A 1237 −11.186 −5.534 −5.491 1.00 1.00 H ATOM 4157 N ASN A 1238 −12.552 −2.944 −2.659 1.00 1.00 N ATOM 4158 CA ASN A 1238 −13.742 −2.410 −1.957 1.00 1.00 C ATOM 4159 C ASN A 1238 −14.921 −2.371 −2.978 1.00 1.00 C ATOM 4160 O ASN A 1238 −14.560 −2.127 −4.103 1.00 1.00 O ATOM 4161 CB ASN A 1238 −13.562 −1.073 −1.161 1.00 1.00 C ATOM 4162 CG ASN A 1238 −12.432 −1.362 −0.176 1.00 1.00 C ATOM 4163 OD1 ASN A 1238 −12.799 −1.584 0.943 1.00 1.00 O ATOM 4164 ND2 ASN A 1238 −11.152 −1.466 −0.574 1.00 1.00 N ATOM 4165 HA ASN A 1238 −14.058 −3.086 −1.142 1.00 1.00 H ATOM 4166 HB1 ASN A 1238 −13.318 −0.228 −1.791 1.00 1.00 H ATOM 4167 HB2 ASN A 1238 −14.463 −0.811 −0.587 1.00 1.00 H ATOM 4168 HD22 ASN A 1238 −10.447 −1.762 0.103 1.00 1.00 H ATOM 4169 HD21 ASN A 1238 −10.906 −1.245 −1.501 1.00 1.00 H ATOM 4170 HN ASN A 1238 −12.107 −2.391 −3.383 1.00 1.00 H ATOM 4171 N LYS A 1239 −16.247 −2.584 −2.682 1.00 1.00 N ATOM 4172 CA LYS A 1239 −17.163 −2.868 −3.772 1.00 1.00 C ATOM 4173 C LYS A 1239 −18.635 −2.853 −3.476 1.00 1.00 C ATOM 4174 O LYS A 1239 −18.991 −2.995 −2.296 1.00 1.00 O ATOM 4175 CB LYS A 1239 −16.806 −4.258 −4.348 1.00 1.00 C ATOM 4176 CG LYS A 1239 −16.673 −5.523 −3.370 1.00 1.00 C ATOM 4177 CD LYS A 1239 −15.569 −5.468 −2.248 1.00 1.00 C ATOM 4178 CE LYS A 1239 −15.228 −6.838 −1.584 1.00 1.00 C ATOM 4179 NZ LYS A 1239 −14.107 −6.804 −0.652 1.00 1.00 N ATOM 4180 HA LYS A 1239 −16.980 −2.051 −4.514 1.00 1.00 H ATOM 4181 HB1 LYS A 1239 −17.515 −4.487 −5.152 1.00 1.00 H ATOM 4182 HB2 LYS A 1239 −15.857 −4.153 −4.905 1.00 1.00 H ATOM 4183 HG1 LYS A 1239 −16.449 −6.391 −3.995 1.00 1.00 H ATOM 4184 HG2 LYS A 1239 −17.625 −5.775 −2.904 1.00 1.00 H ATOM 4185 HD1 LYS A 1239 −14.740 −5.012 −2.754 1.00 1.00 H ATOM 4186 HD2 LYS A 1239 −15.937 −4.759 −1.454 1.00 1.00 H ATOM 4187 HE1 LYS A 1239 −16.142 −7.224 −1.134 1.00 1.00 H ATOM 4188 HE2 LYS A 1239 −15.008 −7.473 −2.440 1.00 1.00 H ATOM 4189 HZ1 LYS A 1239 −13.764 −7.746 −0.359 1.00 1.00 H ATOM 4190 HZ2 LYS A 1239 −14.092 −6.226 0.290 1.00 1.00 H ATOM 4191 HZ3 LYS A 1239 −13.210 −6.403 −1.055 1.00 1.00 H ATOM 4192 HN LYS A 1239 −16.575 −2.542 −1.738 1.00 1.00 H ATOM 4193 N THR A 1240 −19.502 −2.760 −4.544 1.00 1.00 N ATOM 4194 CA THR A 1240 −20.962 −2.921 −4.434 1.00 1.00 C ATOM 4195 C THR A 1240 −21.466 −3.518 −5.710 1.00 1.00 C ATOM 4196 O THR A 1240 −20.897 −3.145 −6.716 1.00 1.00 O ATOM 4197 CB THR A 1240 −21.694 −1.556 −4.131 1.00 1.00 C ATOM 4198 OG1 THR A 1240 −20.921 −0.803 −3.183 1.00 1.00 O ATOM 4199 CG2 THR A 1240 −23.054 −1.811 −3.472 1.00 1.00 C ATOM 4200 HA THR A 1240 −21.137 −3.624 −3.640 1.00 1.00 H ATOM 4201 HB THR A 1240 −21.789 −0.921 −5.077 1.00 1.00 H ATOM 4202 HG1 THR A 1240 −20.702 −1.250 −2.359 1.00 1.00 H ATOM 4203 HG23 THR A 1240 −23.501 −0.946 −3.009 1.00 1.00 H ATOM 4204 HG21 THR A 1240 −23.775 −2.232 −4.161 1.00 1.00 H ATOM 4205 HG22 THR A 1240 −22.959 −2.511 −2.612 1.00 1.00 H ATOM 4206 HN THR A 1240 −19.124 −2.640 −5.465 1.00 1.00 H ATOM 4207 N LYS A 1241 −22.450 −4.502 −5.645 1.00 1.00 N ATOM 4208 CA LYS A 1241 −22.675 −5.354 −6.833 1.00 1.00 C ATOM 4209 C LYS A 1241 −24.155 −5.567 −7.143 1.00 1.00 C ATOM 4210 O LYS A 1241 −24.677 −6.407 −6.422 1.00 1.00 O ATOM 4211 CB LYS A 1241 −21.907 −6.590 −6.372 1.00 1.00 C ATOM 4212 CG LYS A 1241 −21.544 −7.632 −7.481 1.00 1.00 C ATOM 4213 CD LYS A 1241 −22.838 −8.375 −7.998 1.00 1.00 C ATOM 4214 CE LYS A 1241 −22.532 −9.456 −9.033 1.00 1.00 C ATOM 4215 NZ LYS A 1241 −23.724 −9.964 −9.718 1.00 1.00 N ATOM 4216 HA LYS A 1241 −22.157 −4.965 −7.740 1.00 1.00 H ATOM 4217 HB1 LYS A 1241 −22.349 −7.064 −5.481 1.00 1.00 H ATOM 4218 HB2 LYS A 1241 −20.925 −6.292 −6.052 1.00 1.00 H ATOM 4219 HG1 LYS A 1241 −21.086 −7.129 −8.300 1.00 1.00 H ATOM 4220 HG2 LYS A 1241 −20.841 −8.340 −7.082 1.00 1.00 H ATOM 4221 HD1 LYS A 1241 −23.490 −8.798 −7.202 1.00 1.00 H ATOM 4222 HD2 LYS A 1241 −23.433 −7.649 −8.594 1.00 1.00 H ATOM 4223 HE1 LYS A 1241 −21.835 −8.994 −9.776 1.00 1.00 H ATOM 4224 HE2 LYS A 1241 −22.071 −10.339 −8.609 1.00 1.00 H ATOM 4225 HZ1 LYS A 1241 −24.221 −9.304 −10.401 1.00 1.00 H ATOM 4226 HZ2 LYS A 1241 −23.498 −10.771 −10.453 1.00 1.00 H ATOM 4227 HZ3 LYS A 1241 −24.507 −10.477 −9.197 1.00 1.00 H ATOM 4228 HN LYS A 1241 −22.946 −4.719 −4.759 1.00 1.00 H ATOM 4229 N ARG A 1242 −24.781 −4.811 −8.097 1.00 1.00 N ATOM 4230 CA ARG A 1242 −26.219 −5.111 −8.334 1.00 1.00 C ATOM 4231 C ARG A 1242 −27.190 −5.242 −7.203 1.00 1.00 C ATOM 4232 O ARG A 1242 −28.052 −4.368 −7.139 1.00 1.00 O ATOM 4233 CB ARG A 1242 −26.148 −6.431 −9.171 1.00 1.00 C ATOM 4234 CG ARG A 1242 −27.596 −6.807 −9.648 1.00 1.00 C ATOM 4235 CD ARG A 1242 −27.651 −8.073 −10.541 1.00 1.00 C ATOM 4236 NE ARG A 1242 −28.913 −8.123 −11.401 1.00 1.00 N ATOM 4237 CZ ARG A 1242 −29.148 −9.130 −12.225 1.00 1.00 C ATOM 4238 NH1 ARG A 1242 −28.323 −10.109 −12.472 1.00 1.00 N ATOM 4239 NH2 ARG A 1242 −30.330 −9.078 −12.848 1.00 1.00 N ATOM 4240 HA ARG A 1242 −26.603 −4.383 −9.047 1.00 1.00 H ATOM 4241 HB1 ARG A 1242 −25.812 −7.324 −8.584 1.00 1.00 H ATOM 4242 HB2 ARG A 1242 −25.427 −6.248 −9.947 1.00 1.00 H ATOM 4243 HG1 ARG A 1242 −28.384 −6.993 −8.845 1.00 1.00 H ATOM 4244 HG2 ARG A 1242 −27.900 −6.016 −10.267 1.00 1.00 H ATOM 4245 HD1 ARG A 1242 −26.762 −8.037 −11.176 1.00 1.00 H ATOM 4246 HD2 ARG A 1242 −27.479 −8.985 −9.945 1.00 1.00 H ATOM 4247 HE ARG A 1242 −29.596 −7.365 −11.340 1.00 1.00 H ATOM 4248 HH12 ARG A 1242 −28.566 −10.827 −13.161 1.00 1.00 H ATOM 4249 HH11 ARG A 1242 −27.432 −10.174 −11.969 1.00 1.00 H ATOM 4250 HH22 ARG A 1242 −30.593 −9.809 −13.564 1.00 1.00 H ATOM 4251 HH21 ARG A 1242 −31.013 −8.355 −12.607 1.00 1.00 H ATOM 4252 HN ARG A 1242 −24.367 −4.132 −8.622 1.00 1.00 H ATOM 4253 N TRP A 1243 −27.177 −6.290 −6.378 1.00 1.00 N ATOM 4254 CA TRP A 1243 −28.386 −6.555 −5.592 1.00 1.00 C ATOM 4255 C TRP A 1243 −28.556 −5.409 −4.649 1.00 1.00 C ATOM 4256 O TRP A 1243 −27.551 −4.969 −4.121 1.00 1.00 O ATOM 4257 CB TRP A 1243 −28.297 −7.951 −4.905 1.00 1.00 C ATOM 4258 CG TRP A 1243 −27.954 −8.978 −5.907 1.00 1.00 C ATOM 4259 CD1 TRP A 1243 −26.818 −9.698 −5.971 1.00 1.00 C ATOM 4260 CD2 TRP A 1243 −28.767 −9.443 −7.095 1.00 1.00 C ATOM 4261 NE1 TRP A 1243 −26.892 −10.545 −6.928 1.00 1.00 N ATOM 4262 CE2 TRP A 1243 −28.002 −10.419 −7.617 1.00 1.00 C ATOM 4263 CE3 TRP A 1243 −29.949 −9.056 −7.694 1.00 1.00 C ATOM 4264 CZ2 TRP A 1243 −28.340 −11.191 −8.704 1.00 1.00 C ATOM 4265 CZ3 TRP A 1243 −30.327 −9.787 −8.827 1.00 1.00 C ATOM 4266 CH2 TRP A 1243 −29.568 −10.890 −9.303 1.00 1.00 C ATOM 4267 HA TRP A 1243 −29.235 −6.508 −6.219 1.00 1.00 H ATOM 4268 HB1 TRP A 1243 −27.396 −7.882 −4.249 1.00 1.00 H ATOM 4269 HB2 TRP A 1243 −29.169 −8.158 −4.255 1.00 1.00 H ATOM 4270 HE1 TRP A 1243 −26.198 −11.272 −7.095 1.00 1.00 H ATOM 4271 HD1 TRP A 1243 −25.930 −9.600 −5.341 1.00 1.00 H ATOM 4272 HZ2 TRP A 1243 −27.714 −12.008 −9.043 1.00 1.00 H ATOM 4273 HH2 TRP A 1243 −29.970 −11.509 −10.097 1.00 1.00 H ATOM 4274 HZ3 TRP A 1243 −31.204 −9.581 −9.356 1.00 1.00 H ATOM 4275 HE3 TRP A 1243 −30.545 −8.254 −7.291 1.00 1.00 H ATOM 4276 HN TRP A 1243 −26.408 −6.874 −6.260 1.00 1.00 H ATOM 4277 N GLY A 1244 −29.808 −4.876 −4.476 1.00 1.00 N ATOM 4278 CA GLY A 1244 −29.978 −3.608 −3.779 1.00 1.00 C ATOM 4279 C GLY A 1244 −29.944 −2.412 −4.717 1.00 1.00 C ATOM 4280 O GLY A 1244 −30.594 −1.434 −4.354 1.00 1.00 O ATOM 4281 HA2 GLY A 1244 −29.200 −3.437 −2.975 1.00 1.00 H ATOM 4282 HA1 GLY A 1244 −30.960 −3.667 −3.268 1.00 1.00 H ATOM 4283 HN GLY A 1244 −30.615 −5.277 −4.904 1.00 1.00 H ATOM 4284 N TYR A 1245 −29.193 −2.386 −5.863 1.00 1.00 N ATOM 4285 CA TYR A 1245 −29.274 −1.212 −6.730 1.00 1.00 C ATOM 4286 C TYR A 1245 −28.841 0.009 −5.916 1.00 1.00 C ATOM 4287 O TYR A 1245 −29.394 1.024 −6.202 1.00 1.00 O ATOM 4288 CB TYR A 1245 −30.636 −1.225 −7.573 1.00 1.00 C ATOM 4289 CG TYR A 1245 −30.680 −2.567 −8.351 1.00 1.00 C ATOM 4290 CD1 TYR A 1245 −30.096 −2.590 −9.604 1.00 1.00 C ATOM 4291 CD2 TYR A 1245 −31.248 −3.693 −7.734 1.00 1.00 C ATOM 4292 CE1 TYR A 1245 −30.137 −3.759 −10.331 1.00 1.00 C ATOM 4293 CE2 TYR A 1245 −31.309 −4.875 −8.508 1.00 1.00 C ATOM 4294 CZ TYR A 1245 −30.755 −4.901 −9.797 1.00 1.00 C ATOM 4295 OH TYR A 1245 −30.806 −6.088 −10.524 1.00 1.00 O ATOM 4296 HA TYR A 1245 −28.436 −1.412 −7.394 1.00 1.00 H ATOM 4297 HB2 TYR A 1245 −31.572 −1.109 −6.910 1.00 1.00 H ATOM 4298 HB1 TYR A 1245 −30.655 −0.425 −8.306 1.00 1.00 H ATOM 4299 HD2 TYR A 1245 −31.677 −3.706 −6.753 1.00 1.00 H ATOM 4300 HE2 TYR A 1245 −31.817 −5.741 −8.186 1.00 1.00 H ATOM 4301 HE1 TYR A 1245 −29.657 −3.801 −11.325 1.00 1.00 H ATOM 4302 HD1 TYR A 1245 −29.553 −1.738 −9.975 1.00 1.00 H ATOM 4303 HH TYR A 1245 −31.567 −6.027 −11.096 1.00 1.00 H ATOM 4304 HN TYR A 1245 −28.632 −3.158 −6.228 1.00 1.00 H ATOM 4305 N SER A 1246 −27.911 −0.129 −4.938 1.00 1.00 N ATOM 4306 CA SER A 1246 −27.437 0.959 −4.083 1.00 1.00 C ATOM 4307 C SER A 1246 −25.950 1.057 −4.346 1.00 1.00 C ATOM 4308 O SER A 1246 −25.128 0.813 −3.465 1.00 1.00 O ATOM 4309 CB SER A 1246 −27.670 0.502 −2.614 1.00 1.00 C ATOM 4310 OG SER A 1246 −26.887 −0.682 −2.295 1.00 1.00 O ATOM 4311 HA SER A 1246 −27.951 1.952 −4.288 1.00 1.00 H ATOM 4312 HB1 SER A 1246 −27.425 1.364 −1.959 1.00 1.00 H ATOM 4313 HB2 SER A 1246 −28.712 0.209 −2.522 1.00 1.00 H ATOM 4314 HG SER A 1246 −25.976 −0.461 −2.327 1.00 1.00 H ATOM 4315 HN SER A 1246 −27.528 −1.052 −4.743 1.00 1.00 H ATOM 4316 N LEU A 1247 −25.584 1.399 −5.608 1.00 1.00 N ATOM 4317 CA LEU A 1247 −24.202 1.437 −6.027 1.00 1.00 C ATOM 4318 C LEU A 1247 −23.564 2.809 −5.582 1.00 1.00 C ATOM 4319 O LEU A 1247 −23.796 3.800 −6.276 1.00 1.00 O ATOM 4320 CB LEU A 1247 −24.107 1.221 −7.583 1.00 1.00 C ATOM 4321 CG LEU A 1247 −24.394 −0.264 −8.053 1.00 1.00 C ATOM 4322 CD1 LEU A 1247 −23.403 −1.201 −7.343 1.00 1.00 C ATOM 4323 CD2 LEU A 1247 −25.805 −0.775 −7.836 1.00 1.00 C ATOM 4324 HA LEU A 1247 −23.565 0.734 −5.458 1.00 1.00 H ATOM 4325 HB1 LEU A 1247 −23.154 1.605 −7.979 1.00 1.00 H ATOM 4326 HB2 LEU A 1247 −24.920 1.759 −8.031 1.00 1.00 H ATOM 4327 HG LEU A 1247 −24.123 −0.185 −9.136 1.00 1.00 H ATOM 4328 HD21 LEU A 1247 −26.431 0.029 −8.257 1.00 1.00 H ATOM 4329 HD22 LEU A 1247 −26.050 −1.723 −8.325 1.00 1.00 H ATOM 4330 HD23 LEU A 1247 −26.110 −0.909 −6.785 1.00 1.00 H ATOM 4331 HD11 LEU A 1247 −23.714 −1.322 −6.294 1.00 1.00 H ATOM 4332 HD12 LEU A 1247 −23.401 −2.198 −7.840 1.00 1.00 H ATOM 4333 HD13 LEU A 1247 −22.328 −0.770 −7.433 1.00 1.00 H ATOM 4334 HN LEU A 1247 −26.204 1.725 −6.260 1.00 1.00 H ATOM 4335 N HIS A 1248 −22.772 2.887 −4.491 1.00 1.00 N ATOM 4336 CA HIS A 1248 −22.075 4.139 −4.277 1.00 1.00 C ATOM 4337 C HIS A 1248 −21.156 4.383 −5.495 1.00 1.00 C ATOM 4338 O HIS A 1248 −20.589 3.384 −5.944 1.00 1.00 O ATOM 4339 CB HIS A 1248 −21.106 4.200 −3.091 1.00 1.00 C ATOM 4340 CG HIS A 1248 −20.120 3.061 −3.041 1.00 1.00 C ATOM 4341 ND1 HIS A 1248 −19.045 3.081 −3.731 1.00 1.00 N ATOM 4342 CD2 HIS A 1248 −20.156 1.951 −2.315 1.00 1.00 C ATOM 4343 CE1 HIS A 1248 −18.294 2.075 −3.480 1.00 1.00 C ATOM 4344 NE2 HIS A 1248 −18.873 1.345 −2.639 1.00 1.00 N ATOM 4345 HA HIS A 1248 −22.739 5.032 −4.178 1.00 1.00 H ATOM 4346 HB1 HIS A 1248 −21.765 4.249 −2.155 1.00 1.00 H ATOM 4347 HB2 HIS A 1248 −20.527 5.131 −3.034 1.00 1.00 H ATOM 4348 HD2 HIS A 1248 −20.953 1.575 −1.634 1.00 1.00 H ATOM 4349 HE1 HIS A 1248 −17.315 1.877 −3.944 1.00 1.00 H ATOM 4350 HD1 HIS A 1248 −18.776 3.809 −4.398 1.00 1.00 H ATOM 4351 HN HIS A 1248 −22.668 2.082 −3.898 1.00 1.00 H ATOM 4352 N PHE A 1249 −20.936 5.662 −6.009 1.00 1.00 N ATOM 4353 CA PHE A 1249 −19.874 5.829 −6.946 1.00 1.00 C ATOM 4354 C PHE A 1249 −19.692 7.291 −7.267 1.00 1.00 C ATOM 4355 O PHE A 1249 −20.633 7.912 −7.709 1.00 1.00 O ATOM 4356 CB PHE A 1249 −20.131 5.138 −8.284 1.00 1.00 C ATOM 4357 CG PHE A 1249 −18.794 4.902 −9.043 1.00 1.00 C ATOM 4358 CD1 PHE A 1249 −17.987 3.792 −8.841 1.00 1.00 C ATOM 4359 CD2 PHE A 1249 −18.355 5.871 −9.935 1.00 1.00 C ATOM 4360 CE1 PHE A 1249 −16.861 3.502 −9.614 1.00 1.00 C ATOM 4361 CE2 PHE A 1249 −17.208 5.611 −10.711 1.00 1.00 C ATOM 4362 CZ PHE A 1249 −16.462 4.442 −10.538 1.00 1.00 C ATOM 4363 HA PHE A 1249 −18.946 5.470 −6.528 1.00 1.00 H ATOM 4364 HB1 PHE A 1249 −20.731 5.863 −8.840 1.00 1.00 H ATOM 4365 HB2 PHE A 1249 −20.724 4.224 −8.227 1.00 1.00 H ATOM 4366 HD2 PHE A 1249 −18.907 6.804 −10.062 1.00 1.00 H ATOM 4367 HE2 PHE A 1249 −16.904 6.251 −11.527 1.00 1.00 H ATOM 4368 HZ PHE A 1249 −15.574 4.264 −11.144 1.00 1.00 H ATOM 4369 HE1 PHE A 1249 −16.311 2.541 −9.516 1.00 1.00 H ATOM 4370 HD1 PHE A 1249 −18.249 3.083 −8.054 1.00 1.00 H ATOM 4371 HN PHE A 1249 −21.488 6.447 −5.732 1.00 1.00 H ATOM 4372 N MET A 1250 −18.503 7.877 −7.118 1.00 1.00 N ATOM 4373 CA MET A 1250 −18.339 9.265 −7.534 1.00 1.00 C ATOM 4374 C MET A 1250 −19.281 10.205 −6.801 1.00 1.00 C ATOM 4375 O MET A 1250 −19.979 11.007 −7.448 1.00 1.00 O ATOM 4376 CB MET A 1250 −18.372 9.462 −9.104 1.00 1.00 C ATOM 4377 CG MET A 1250 −18.009 10.928 −9.503 1.00 1.00 C ATOM 4378 SD MET A 1250 −16.215 11.204 −9.672 1.00 1.00 S ATOM 4379 CE MET A 1250 −16.184 13.079 −9.677 1.00 1.00 C ATOM 4380 HA MET A 1250 −17.387 9.701 −7.175 1.00 1.00 H ATOM 4381 HB1 MET A 1250 −19.372 9.244 −9.441 1.00 1.00 H ATOM 4382 HB2 MET A 1250 −17.652 8.798 −9.561 1.00 1.00 H ATOM 4383 HG1 MET A 1250 −18.459 11.179 −10.463 1.00 1.00 H ATOM 4384 HG2 MET A 1250 −18.242 11.669 −8.753 1.00 1.00 H ATOM 4385 HE1 MET A 1250 −15.101 13.371 −9.847 1.00 1.00 H ATOM 4386 HE2 MET A 1250 −16.615 13.461 −8.731 1.00 1.00 H ATOM 4387 HE3 MET A 1250 −16.746 13.410 −10.633 1.00 1.00 H ATOM 4388 HN MET A 1250 −17.718 7.409 −6.652 1.00 1.00 H ATOM 4389 N GLY A 1251 −19.396 10.213 −5.447 1.00 1.00 N ATOM 4390 CA GLY A 1251 −20.192 11.219 −4.852 1.00 1.00 C ATOM 4391 C GLY A 1251 −21.659 11.161 −5.153 1.00 1.00 C ATOM 4392 O GLY A 1251 −22.387 12.123 −4.910 1.00 1.00 O ATOM 4393 HA2 GLY A 1251 −19.791 12.140 −5.170 1.00 1.00 H ATOM 4394 HA1 GLY A 1251 −20.009 11.053 −3.764 1.00 1.00 H ATOM 4395 HN GLY A 1251 −18.883 9.501 −4.894 1.00 1.00 H ATOM 4396 N TYR A 1252 −22.149 9.968 −5.534 1.00 1.00 N ATOM 4397 CA TYR A 1252 −23.601 9.801 −5.606 1.00 1.00 C ATOM 4398 C TYR A 1252 −23.933 8.329 −5.680 1.00 1.00 C ATOM 4399 O TYR A 1252 −22.975 7.546 −5.532 1.00 1.00 O ATOM 4400 CB TYR A 1252 −24.090 10.628 −6.849 1.00 1.00 C ATOM 4401 CG TYR A 1252 −23.019 10.957 −7.884 1.00 1.00 C ATOM 4402 CD1 TYR A 1252 −22.577 10.008 −8.809 1.00 1.00 C ATOM 4403 CD2 TYR A 1252 −22.383 12.223 −7.898 1.00 1.00 C ATOM 4404 CE1 TYR A 1252 −21.857 10.482 −9.916 1.00 1.00 C ATOM 4405 CE2 TYR A 1252 −21.465 12.588 −8.918 1.00 1.00 C ATOM 4406 CZ TYR A 1252 −21.312 11.771 −10.047 1.00 1.00 C ATOM 4407 OH TYR A 1252 −20.726 12.256 −11.215 1.00 1.00 O ATOM 4408 HA TYR A 1252 −24.126 10.112 −4.676 1.00 1.00 H ATOM 4409 HB2 TYR A 1252 −24.595 11.574 −6.513 1.00 1.00 H ATOM 4410 HB1 TYR A 1252 −24.770 10.028 −7.472 1.00 1.00 H ATOM 4411 HD2 TYR A 1252 −22.703 12.952 −7.119 1.00 1.00 H ATOM 4412 HE2 TYR A 1252 −20.860 13.460 −8.774 1.00 1.00 H ATOM 4413 HE1 TYR A 1252 −21.692 9.832 −10.733 1.00 1.00 H ATOM 4414 HD1 TYR A 1252 −22.788 8.921 −8.684 1.00 1.00 H ATOM 4415 HH TYR A 1252 −20.332 13.125 −11.144 1.00 1.00 H ATOM 4416 HN TYR A 1252 −21.613 9.168 −5.685 1.00 1.00 H ATOM 4417 N VAL A 1253 −25.269 8.018 −5.903 1.00 1.00 N ATOM 4418 CA VAL A 1253 −25.689 6.642 −6.042 1.00 1.00 C ATOM 4419 C VAL A 1253 −25.936 6.342 −7.505 1.00 1.00 C ATOM 4420 O VAL A 1253 −26.500 7.171 −8.157 1.00 1.00 O ATOM 4421 CB VAL A 1253 −27.007 6.334 −5.225 1.00 1.00 C ATOM 4422 CG1 VAL A 1253 −27.240 4.800 −5.238 1.00 1.00 C ATOM 4423 CG2 VAL A 1253 −27.030 6.910 −3.789 1.00 1.00 C ATOM 4424 HA VAL A 1253 −24.928 6.077 −5.621 1.00 1.00 H ATOM 4425 HB VAL A 1253 −27.882 6.796 −5.723 1.00 1.00 H ATOM 4426 HG11 VAL A 1253 −27.293 4.405 −6.224 1.00 1.00 H ATOM 4427 HG12 VAL A 1253 −26.441 4.230 −4.663 1.00 1.00 H ATOM 4428 HG13 VAL A 1253 −28.196 4.596 −4.708 1.00 1.00 H ATOM 4429 HG21 VAL A 1253 −26.910 8.007 −3.800 1.00 1.00 H ATOM 4430 HG22 VAL A 1253 −26.154 6.502 −3.320 1.00 1.00 H ATOM 4431 HG23 VAL A 1253 −27.964 6.640 −3.267 1.00 1.00 H ATOM 4432 HN VAL A 1253 −25.979 8.745 −5.936 1.00 1.00 H ATOM 4433 N ILE A 1254 −25.484 5.191 −8.063 1.00 1.00 N ATOM 4434 CA ILE A 1254 −25.705 4.875 −9.472 1.00 1.00 C ATOM 4435 C ILE A 1254 −26.942 3.962 −9.550 1.00 1.00 C ATOM 4436 O ILE A 1254 −26.880 2.841 −10.051 1.00 1.00 O ATOM 4437 CB ILE A 1254 −24.438 4.381 −10.164 1.00 1.00 C ATOM 4438 CG1 ILE A 1254 −23.231 5.303 −9.905 1.00 1.00 C ATOM 4439 CG2 ILE A 1254 −24.562 3.996 −11.645 1.00 1.00 C ATOM 4440 CD1 ILE A 1254 −23.284 6.580 −10.725 1.00 1.00 C ATOM 4441 HA ILE A 1254 −25.969 5.789 −10.015 1.00 1.00 H ATOM 4442 HB ILE A 1254 −24.182 3.476 −9.604 1.00 1.00 H ATOM 4443 HG11 ILE A 1254 −23.134 5.689 −8.868 1.00 1.00 H ATOM 4444 HG12 ILE A 1254 −22.315 4.734 −10.096 1.00 1.00 H ATOM 4445 HD11 ILE A 1254 −24.172 7.212 −10.418 1.00 1.00 H ATOM 4446 HD12 ILE A 1254 −22.430 7.263 −10.607 1.00 1.00 H ATOM 4447 HD13 ILE A 1254 −23.407 6.348 −11.795 1.00 1.00 H ATOM 4448 HG21 ILE A 1254 −25.049 4.710 −12.331 1.00 1.00 H ATOM 4449 HG22 ILE A 1254 −23.549 3.763 −12.071 1.00 1.00 H ATOM 4450 HG23 ILE A 1254 −25.168 3.055 −11.770 1.00 1.00 H ATOM 4451 HN ILE A 1254 −25.087 4.465 −7.506 1.00 1.00 H ATOM 4452 N GLY A 1255 −28.092 4.483 −9.062 1.00 1.00 N ATOM 4453 CA GLY A 1255 −29.325 3.663 −8.957 1.00 1.00 C ATOM 4454 C GLY A 1255 −30.431 4.538 −8.437 1.00 1.00 C ATOM 4455 O GLY A 1255 −31.519 4.530 −9.005 1.00 1.00 O ATOM 4456 HA2 GLY A 1255 −29.190 2.769 −8.303 1.00 1.00 H ATOM 4457 HA1 GLY A 1255 −29.595 3.325 −9.915 1.00 1.00 H ATOM 4458 HN GLY A 1255 −28.108 5.433 −8.745 1.00 1.00 H ATOM 4459 N CYS A 1256 −30.245 5.355 −7.341 1.00 1.00 N ATOM 4460 CA CYS A 1256 −31.382 6.027 −6.722 1.00 1.00 C ATOM 4461 C CYS A 1256 −31.250 7.538 −6.620 1.00 1.00 C ATOM 4462 O CYS A 1256 −31.571 8.130 −5.595 1.00 1.00 O ATOM 4463 CB CYS A 1256 −31.811 5.452 −5.356 1.00 1.00 C ATOM 4464 SG CYS A 1256 −30.532 5.619 −4.039 1.00 1.00 S ATOM 4465 HA CYS A 1256 −32.209 5.931 −7.410 1.00 1.00 H ATOM 4466 HB1 CYS A 1256 −31.890 4.373 −5.556 1.00 1.00 H ATOM 4467 HB2 CYS A 1256 −32.774 5.819 −4.970 1.00 1.00 H ATOM 4468 HG CYS A 1256 −30.512 6.621 −4.029 1.00 1.00 H ATOM 4469 HN CYS A 1256 −29.418 5.391 −6.833 1.00 1.00 H ATOM 4470 N TYR A 1257 −30.709 8.170 −7.682 1.00 1.00 N ATOM 4471 CA TYR A 1257 −30.564 9.629 −7.705 1.00 1.00 C ATOM 4472 C TYR A 1257 −29.543 10.121 −6.723 1.00 1.00 C ATOM 4473 O TYR A 1257 −28.500 10.598 −7.146 1.00 1.00 O ATOM 4474 CB TYR A 1257 −31.919 10.342 −7.500 1.00 1.00 C ATOM 4475 CG TYR A 1257 −31.797 11.864 −7.577 1.00 1.00 C ATOM 4476 CD1 TYR A 1257 −31.758 12.647 −6.399 1.00 1.00 C ATOM 4477 CD2 TYR A 1257 −31.745 12.544 −8.790 1.00 1.00 C ATOM 4478 CE1 TYR A 1257 −31.523 14.046 −6.421 1.00 1.00 C ATOM 4479 CE2 TYR A 1257 −31.625 13.951 −8.818 1.00 1.00 C ATOM 4480 CZ TYR A 1257 −31.498 14.679 −7.670 1.00 1.00 C ATOM 4481 OH TYR A 1257 −31.310 16.032 −7.730 1.00 1.00 O ATOM 4482 HA TYR A 1257 −30.222 9.938 −8.733 1.00 1.00 H ATOM 4483 HB2 TYR A 1257 −32.573 9.986 −8.268 1.00 1.00 H ATOM 4484 HB1 TYR A 1257 −32.477 10.194 −6.548 1.00 1.00 H ATOM 4485 HD2 TYR A 1257 −31.721 12.005 −9.733 1.00 1.00 H ATOM 4486 HE2 TYR A 1257 −31.601 14.408 −9.765 1.00 1.00 H ATOM 4487 HE1 TYR A 1257 −31.439 14.609 −5.487 1.00 1.00 H ATOM 4488 HD1 TYR A 1257 −31.816 12.167 −5.464 1.00 1.00 H ATOM 4489 HH TYR A 1257 −30.667 16.358 −8.335 1.00 1.00 H ATOM 4490 HN TYR A 1257 −30.440 7.600 −8.494 1.00 1.00 H ATOM 4491 N GLY A 1258 −29.761 10.022 −5.414 1.00 1.00 N ATOM 4492 CA GLY A 1258 −28.692 10.385 −4.448 1.00 1.00 C ATOM 4493 C GLY A 1258 −28.375 11.873 −4.506 1.00 1.00 C ATOM 4494 O GLY A 1258 −28.927 12.584 −3.689 1.00 1.00 O ATOM 4495 HA2 GLY A 1258 −27.792 9.855 −4.748 1.00 1.00 H ATOM 4496 HA1 GLY A 1258 −28.996 10.030 −3.450 1.00 1.00 H ATOM 4497 HN GLY A 1258 −30.604 9.688 −4.997 1.00 1.00 H ATOM 4498 N SER A 1259 −27.499 12.346 −5.411 1.00 1.00 N ATOM 4499 CA SER A 1259 −27.186 13.765 −5.525 1.00 1.00 C ATOM 4500 C SER A 1259 −26.784 14.193 −6.919 1.00 1.00 C ATOM 4501 O SER A 1259 −25.603 14.421 −7.139 1.00 1.00 O ATOM 4502 CB SER A 1259 −26.135 13.929 −4.449 1.00 1.00 C ATOM 4503 OG SER A 1259 −25.726 15.265 −4.261 1.00 1.00 O ATOM 4504 HA SER A 1259 −28.079 14.438 −5.359 1.00 1.00 H ATOM 4505 HB1 SER A 1259 −26.503 13.602 −3.463 1.00 1.00 H ATOM 4506 HB2 SER A 1259 −25.234 13.296 −4.655 1.00 1.00 H ATOM 4507 HG SER A 1259 −24.939 15.400 −3.744 1.00 1.00 H ATOM 4508 HN SER A 1259 −27.031 11.668 −6.025 1.00 1.00 H ATOM 4509 N LEU A 1260 −27.670 14.348 −7.920 1.00 1.00 N ATOM 4510 CA LEU A 1260 −27.251 14.602 −9.326 1.00 1.00 C ATOM 4511 C LEU A 1260 −28.127 15.660 −9.896 1.00 1.00 C ATOM 4512 O LEU A 1260 −29.216 15.837 −9.386 1.00 1.00 O ATOM 4513 CB LEU A 1260 −27.453 13.336 −10.159 1.00 1.00 C ATOM 4514 CG LEU A 1260 −26.534 12.123 −9.882 1.00 1.00 C ATOM 4515 CD1 LEU A 1260 −27.167 10.904 −10.581 1.00 1.00 C ATOM 4516 CD2 LEU A 1260 −25.110 12.492 −10.348 1.00 1.00 C ATOM 4517 HA LEU A 1260 −26.212 14.977 −9.369 1.00 1.00 H ATOM 4518 HB1 LEU A 1260 −28.564 13.101 −10.020 1.00 1.00 H ATOM 4519 HB2 LEU A 1260 −27.309 13.553 −11.214 1.00 1.00 H ATOM 4520 HG LEU A 1260 −26.540 11.924 −8.818 1.00 1.00 H ATOM 4521 HD21 LEU A 1260 −24.410 11.696 −10.307 1.00 1.00 H ATOM 4522 HD22 LEU A 1260 −25.069 12.762 −11.373 1.00 1.00 H ATOM 4523 HD23 LEU A 1260 −24.772 13.333 −9.756 1.00 1.00 H ATOM 4524 HD11 LEU A 1260 −28.170 10.665 −10.168 1.00 1.00 H ATOM 4525 HD12 LEU A 1260 −26.527 10.065 −10.283 1.00 1.00 H ATOM 4526 HD13 LEU A 1260 −27.241 11.095 −11.641 1.00 1.00 H ATOM 4527 HN LEU A 1260 −28.633 14.171 −7.833 1.00 1.00 H ATOM 4528 N PRO A 1261 −27.729 16.463 −10.910 1.00 1.00 N ATOM 4529 CA PRO A 1261 −26.389 16.398 −11.523 1.00 1.00 C ATOM 4530 C PRO A 1261 −25.454 17.204 −10.656 1.00 1.00 C ATOM 4531 O PRO A 1261 −25.834 18.231 −10.072 1.00 1.00 O ATOM 4532 CB PRO A 1261 −26.611 17.107 −12.864 1.00 1.00 C ATOM 4533 CG PRO A 1261 −27.849 18.026 −12.657 1.00 1.00 C ATOM 4534 CD PRO A 1261 −28.726 17.329 −11.559 1.00 1.00 C ATOM 4535 HA PRO A 1261 −26.055 15.320 −11.752 1.00 1.00 H ATOM 4536 HD2 PRO A 1261 −29.537 16.707 −12.022 1.00 1.00 H ATOM 4537 HD1 PRO A 1261 −29.206 18.072 −10.907 1.00 1.00 H ATOM 4538 HG2 PRO A 1261 −28.450 18.046 −13.575 1.00 1.00 H ATOM 4539 HG1 PRO A 1261 −27.584 19.051 −12.393 1.00 1.00 H ATOM 4540 HB1 PRO A 1261 −25.760 17.687 −13.203 1.00 1.00 H ATOM 4541 HB2 PRO A 1261 −26.854 16.363 −13.671 1.00 1.00 H ATOM 4542 N GLN A 1262 −24.188 16.742 −10.523 1.00 1.00 N ATOM 4543 CA GLN A 1262 −23.280 17.386 −9.557 1.00 1.00 C ATOM 4544 C GLN A 1262 −23.026 18.855 −9.780 1.00 1.00 C ATOM 4545 O GLN A 1262 −22.852 19.633 −8.842 1.00 1.00 O ATOM 4546 CB GLN A 1262 −21.890 16.651 −9.382 1.00 1.00 C ATOM 4547 CG GLN A 1262 −21.004 16.730 −10.669 1.00 1.00 C ATOM 4548 CD GLN A 1262 −19.784 15.823 −10.614 1.00 1.00 C ATOM 4549 OE1 GLN A 1262 −19.827 14.828 −11.314 1.00 1.00 O ATOM 4550 NE2 GLN A 1262 −18.763 16.037 −9.749 1.00 1.00 N ATOM 4551 HA GLN A 1262 −23.791 17.276 −8.589 1.00 1.00 H ATOM 4552 HB1 GLN A 1262 −21.373 17.172 −8.526 1.00 1.00 H ATOM 4553 HB2 GLN A 1262 −22.153 15.577 −9.144 1.00 1.00 H ATOM 4554 HG1 GLN A 1262 −21.587 16.531 −11.641 1.00 1.00 H ATOM 4555 HG2 GLN A 1262 −20.612 17.761 −10.724 1.00 1.00 H ATOM 4556 HE22 GLN A 1262 −17.960 15.420 −9.706 1.00 1.00 H ATOM 4557 HE21 GLN A 1262 −18.885 16.778 −9.043 1.00 1.00 H ATOM 4558 HN GLN A 1262 −23.904 15.893 −10.973 1.00 1.00 H ATOM 4559 N ASP A 1263 −23.099 19.292 −11.079 1.00 1.00 N ATOM 4560 CA ASP A 1263 −22.915 20.739 −11.346 1.00 1.00 C ATOM 4561 C ASP A 1263 −23.983 21.438 −10.492 1.00 1.00 C ATOM 4562 O ASP A 1263 −23.726 22.359 −9.720 1.00 1.00 O ATOM 4563 CB ASP A 1263 −23.033 21.137 −12.797 1.00 1.00 C ATOM 4564 CG ASP A 1263 −22.690 22.569 −12.921 1.00 1.00 C ATOM 4565 OD1 ASP A 1263 −23.240 23.312 −13.738 1.00 1.00 O ATOM 4566 OD2 ASP A 1263 −21.842 23.056 −12.148 1.00 1.00 O ATOM 4567 HA ASP A 1263 −21.915 21.048 −11.048 1.00 1.00 H ATOM 4568 HB1 ASP A 1263 −22.359 20.439 −13.333 1.00 1.00 H ATOM 4569 HB2 ASP A 1263 −24.061 20.949 −13.100 1.00 1.00 H ATOM 4570 HN ASP A 1263 −23.278 18.674 −11.837 1.00 1.00 H ATOM 4571 N HIS A 1264 −25.253 21.014 −10.578 1.00 1.00 N ATOM 4572 CA HIS A 1264 −26.330 21.704 −9.848 1.00 1.00 C ATOM 4573 C HIS A 1264 −26.414 21.361 −8.355 1.00 1.00 C ATOM 4574 O HIS A 1264 −26.275 22.238 −7.541 1.00 1.00 O ATOM 4575 CB HIS A 1264 −27.701 21.563 −10.568 1.00 1.00 C ATOM 4576 CG HIS A 1264 −27.785 21.939 −12.052 1.00 1.00 C ATOM 4577 ND1 HIS A 1264 −28.864 21.843 −12.795 1.00 1.00 N ATOM 4578 CD2 HIS A 1264 −26.768 22.481 −12.744 1.00 1.00 C ATOM 4579 CE1 HIS A 1264 −28.615 22.288 −13.967 1.00 1.00 C ATOM 4580 NE2 HIS A 1264 −27.424 22.647 −14.014 1.00 1.00 N ATOM 4581 HA HIS A 1264 −26.226 22.792 −10.009 1.00 1.00 H ATOM 4582 HB1 HIS A 1264 −28.105 20.567 −10.516 1.00 1.00 H ATOM 4583 HB2 HIS A 1264 −28.460 22.183 −10.057 1.00 1.00 H ATOM 4584 HD2 HIS A 1264 −25.789 22.754 −12.534 1.00 1.00 H ATOM 4585 HE1 HIS A 1264 −29.180 22.471 −14.844 1.00 1.00 H ATOM 4586 HD1 HIS A 1264 −29.741 21.436 −12.473 1.00 1.00 H ATOM 4587 HN HIS A 1264 −25.485 20.235 −11.157 1.00 1.00 H ATOM 4588 N ILE A 1265 −26.756 20.088 −8.011 1.00 1.00 N ATOM 4589 CA ILE A 1265 −27.074 19.753 −6.596 1.00 1.00 C ATOM 4590 C ILE A 1265 −25.791 19.433 −5.755 1.00 1.00 C ATOM 4591 O ILE A 1265 −25.956 18.986 −4.623 1.00 1.00 O ATOM 4592 CB ILE A 1265 −28.145 18.576 −6.535 1.00 1.00 C ATOM 4593 CG1 ILE A 1265 −28.878 18.641 −5.160 1.00 1.00 C ATOM 4594 CG2 ILE A 1265 −27.527 17.186 −6.849 1.00 1.00 C ATOM 4595 CD1 ILE A 1265 −29.984 17.571 −5.136 1.00 1.00 C ATOM 4596 HA ILE A 1265 −27.555 20.668 −6.132 1.00 1.00 H ATOM 4597 HB ILE A 1265 −28.842 18.816 −7.332 1.00 1.00 H ATOM 4598 HG11 ILE A 1265 −28.222 18.343 −4.283 1.00 1.00 H ATOM 4599 HG12 ILE A 1265 −29.285 19.621 −4.927 1.00 1.00 H ATOM 4600 HD11 ILE A 1265 −30.563 17.540 −4.183 1.00 1.00 H ATOM 4601 HD12 ILE A 1265 −30.678 17.779 −5.947 1.00 1.00 H ATOM 4602 HD13 ILE A 1265 −29.572 16.577 −5.395 1.00 1.00 H ATOM 4603 HG21 ILE A 1265 −27.151 16.741 −5.952 1.00 1.00 H ATOM 4604 HG22 ILE A 1265 −28.329 16.640 −7.355 1.00 1.00 H ATOM 4605 HG23 ILE A 1265 −26.716 17.395 −7.579 1.00 1.00 H ATOM 4606 HN ILE A 1265 −26.753 19.377 −8.699 1.00 1.00 H ATOM 4607 N ILE A 1266 −24.576 19.767 −6.300 1.00 1.00 N ATOM 4608 CA ILE A 1266 −23.394 19.877 −5.494 1.00 1.00 C ATOM 4609 C ILE A 1266 −22.687 21.188 −5.757 1.00 1.00 C ATOM 4610 O ILE A 1266 −22.428 21.904 −4.809 1.00 1.00 O ATOM 4611 CB ILE A 1266 −22.313 18.730 −5.593 1.00 1.00 C ATOM 4612 CG1 ILE A 1266 −23.000 17.416 −5.240 1.00 1.00 C ATOM 4613 CG2 ILE A 1266 −21.076 19.059 −4.673 1.00 1.00 C ATOM 4614 CD1 ILE A 1266 −22.118 16.139 −5.224 1.00 1.00 C ATOM 4615 HA ILE A 1266 −23.680 19.931 −4.466 1.00 1.00 H ATOM 4616 HB ILE A 1266 −21.833 18.720 −6.591 1.00 1.00 H ATOM 4617 HG11 ILE A 1266 −23.452 17.489 −4.219 1.00 1.00 H ATOM 4618 HG12 ILE A 1266 −23.837 17.199 −5.904 1.00 1.00 H ATOM 4619 HD11 ILE A 1266 −21.575 16.062 −6.151 1.00 1.00 H ATOM 4620 HD12 ILE A 1266 −21.409 16.196 −4.393 1.00 1.00 H ATOM 4621 HD13 ILE A 1266 −22.824 15.284 −5.074 1.00 1.00 H ATOM 4622 HG21 ILE A 1266 −20.327 18.235 −4.775 1.00 1.00 H ATOM 4623 HG22 ILE A 1266 −20.522 19.980 −4.891 1.00 1.00 H ATOM 4624 HG23 ILE A 1266 −21.490 19.157 −3.669 1.00 1.00 H ATOM 4625 HN ILE A 1266 −24.454 20.019 −7.282 1.00 1.00 H ATOM 4626 N GLN A 1267 −22.348 21.576 −7.045 1.00 1.00 N ATOM 4627 CA GLN A 1267 −21.567 22.786 −7.244 1.00 1.00 C ATOM 4628 C GLN A 1267 −22.368 24.018 −7.125 1.00 1.00 C ATOM 4629 O GLN A 1267 −21.944 24.996 −6.479 1.00 1.00 O ATOM 4630 CB GLN A 1267 −20.708 22.772 −8.553 1.00 1.00 C ATOM 4631 CG GLN A 1267 −19.626 21.634 −8.437 1.00 1.00 C ATOM 4632 CD GLN A 1267 −18.789 21.975 −7.231 1.00 1.00 C ATOM 4633 OE1 GLN A 1267 −18.459 23.122 −7.041 1.00 1.00 O ATOM 4634 NE2 GLN A 1267 −18.464 21.005 −6.337 1.00 1.00 N ATOM 4635 HA GLN A 1267 −20.919 22.842 −6.410 1.00 1.00 H ATOM 4636 HB1 GLN A 1267 −21.265 22.528 −9.441 1.00 1.00 H ATOM 4637 HB2 GLN A 1267 −20.177 23.704 −8.782 1.00 1.00 H ATOM 4638 HG1 GLN A 1267 −20.115 20.664 −8.294 1.00 1.00 H ATOM 4639 HG2 GLN A 1267 −19.032 21.526 −9.379 1.00 1.00 H ATOM 4640 HE22 GLN A 1267 −17.946 21.314 −5.553 1.00 1.00 H ATOM 4641 HE21 GLN A 1267 −18.690 20.022 −6.416 1.00 1.00 H ATOM 4642 HN GLN A 1267 −22.537 21.007 −7.827 1.00 1.00 H ATOM 4643 N LYS A 1268 −23.614 24.109 −7.736 1.00 1.00 N ATOM 4644 CA LYS A 1268 −24.357 25.351 −7.569 1.00 1.00 C ATOM 4645 C LYS A 1268 −24.857 25.458 −6.151 1.00 1.00 C ATOM 4646 O LYS A 1268 −24.789 26.481 −5.511 1.00 1.00 O ATOM 4647 CB LYS A 1268 −25.425 25.527 −8.724 1.00 1.00 C ATOM 4648 CG LYS A 1268 −24.847 26.163 −10.048 1.00 1.00 C ATOM 4649 CD LYS A 1268 −23.759 25.354 −10.762 1.00 1.00 C ATOM 4650 CE LYS A 1268 −23.152 26.182 −11.950 1.00 1.00 C ATOM 4651 NZ LYS A 1268 −22.147 25.335 −12.718 1.00 1.00 N ATOM 4652 HA LYS A 1268 −23.745 26.170 −7.689 1.00 1.00 H ATOM 4653 HB1 LYS A 1268 −25.957 24.564 −8.808 1.00 1.00 H ATOM 4654 HB2 LYS A 1268 −26.193 26.274 −8.333 1.00 1.00 H ATOM 4655 HG1 LYS A 1268 −25.689 26.211 −10.742 1.00 1.00 H ATOM 4656 HG2 LYS A 1268 −24.533 27.183 −9.906 1.00 1.00 H ATOM 4657 HD1 LYS A 1268 −23.018 25.071 −10.011 1.00 1.00 H ATOM 4658 HD2 LYS A 1268 −24.142 24.415 −11.186 1.00 1.00 H ATOM 4659 HE1 LYS A 1268 −23.990 26.514 −12.597 1.00 1.00 H ATOM 4660 HE2 LYS A 1268 −22.684 27.098 −11.586 1.00 1.00 H ATOM 4661 HZ1 LYS A 1268 −21.538 24.673 −12.118 1.00 1.00 H ATOM 4662 HZ2 LYS A 1268 −22.571 24.768 −13.502 1.00 1.00 H ATOM 4663 HZ3 LYS A 1268 −21.373 26.022 −13.128 1.00 1.00 H ATOM 4664 HN LYS A 1268 −23.953 23.326 −8.303 1.00 1.00 H ATOM 4665 N ILE A 1269 −25.405 24.379 −5.510 1.00 1.00 N ATOM 4666 CA ILE A 1269 −25.536 24.397 −4.075 1.00 1.00 C ATOM 4667 C ILE A 1269 −24.207 24.774 −3.362 1.00 1.00 C ATOM 4668 O ILE A 1269 −24.263 25.511 −2.388 1.00 1.00 O ATOM 4669 CB ILE A 1269 −26.398 23.233 −3.442 1.00 1.00 C ATOM 4670 CG1 ILE A 1269 −25.644 21.926 −3.454 1.00 1.00 C ATOM 4671 CG2 ILE A 1269 −27.807 23.040 −3.988 1.00 1.00 C ATOM 4672 CD1 ILE A 1269 −26.489 20.824 −2.726 1.00 1.00 C ATOM 4673 HA ILE A 1269 −26.219 25.238 −3.847 1.00 1.00 H ATOM 4674 HB ILE A 1269 −26.524 23.472 −2.357 1.00 1.00 H ATOM 4675 HG11 ILE A 1269 −25.476 21.677 −4.494 1.00 1.00 H ATOM 4676 HG12 ILE A 1269 −24.670 22.106 −2.995 1.00 1.00 H ATOM 4677 HD11 ILE A 1269 −27.290 20.427 −3.327 1.00 1.00 H ATOM 4678 HD12 ILE A 1269 −25.856 20.001 −2.525 1.00 1.00 H ATOM 4679 HD13 ILE A 1269 −26.893 21.125 −1.724 1.00 1.00 H ATOM 4680 HG21 ILE A 1269 −27.645 22.850 −5.051 1.00 1.00 H ATOM 4681 HG22 ILE A 1269 −28.453 22.275 −3.523 1.00 1.00 H ATOM 4682 HG23 ILE A 1269 −28.310 23.987 −3.895 1.00 1.00 H ATOM 4683 HN ILE A 1269 −25.572 23.569 −6.085 1.00 1.00 H ATOM 4684 N LYS A 1270 −22.998 24.367 −3.808 1.00 1.00 N ATOM 4685 CA LYS A 1270 −21.745 24.846 −3.219 1.00 1.00 C ATOM 4686 C LYS A 1270 −21.699 26.323 −3.332 1.00 1.00 C ATOM 4687 O LYS A 1270 −21.368 27.008 −2.367 1.00 1.00 O ATOM 4688 CB LYS A 1270 −20.488 24.170 −3.815 1.00 1.00 C ATOM 4689 CG LYS A 1270 −19.062 24.642 −3.403 1.00 1.00 C ATOM 4690 CD LYS A 1270 −18.692 26.089 −3.852 1.00 1.00 C ATOM 4691 CE LYS A 1270 −18.816 26.359 −5.398 1.00 1.00 C ATOM 4692 NZ LYS A 1270 −17.843 25.701 −6.342 1.00 1.00 N ATOM 4693 HA LYS A 1270 −21.706 24.621 −2.133 1.00 1.00 H ATOM 4694 HB1 LYS A 1270 −20.529 23.122 −3.480 1.00 1.00 H ATOM 4695 HB2 LYS A 1270 −20.388 24.144 −4.864 1.00 1.00 H ATOM 4696 HG1 LYS A 1270 −18.876 24.479 −2.314 1.00 1.00 H ATOM 4697 HG2 LYS A 1270 −18.323 24.018 −3.912 1.00 1.00 H ATOM 4698 HD1 LYS A 1270 −19.276 26.822 −3.296 1.00 1.00 H ATOM 4699 HD2 LYS A 1270 −17.622 26.268 −3.540 1.00 1.00 H ATOM 4700 HE1 LYS A 1270 −19.788 26.149 −5.863 1.00 1.00 H ATOM 4701 HE2 LYS A 1270 −18.721 27.447 −5.542 1.00 1.00 H ATOM 4702 HZ1 LYS A 1270 −17.731 26.159 −7.315 1.00 1.00 H ATOM 4703 HZ2 LYS A 1270 −16.873 25.946 −6.065 1.00 1.00 H ATOM 4704 HZ3 LYS A 1270 −17.841 24.633 −6.358 1.00 1.00 H ATOM 4705 HN LYS A 1270 −22.915 23.714 −4.596 1.00 1.00 H ATOM 4706 N GLU A 1271 −22.134 26.979 −4.458 1.00 1.00 N ATOM 4707 CA GLU A 1271 −22.408 28.402 −4.462 1.00 1.00 C ATOM 4708 C GLU A 1271 −23.162 28.805 −3.230 1.00 1.00 C ATOM 4709 O GLU A 1271 −22.599 29.692 −2.598 1.00 1.00 O ATOM 4710 CB GLU A 1271 −22.928 29.016 −5.806 1.00 1.00 C ATOM 4711 CG GLU A 1271 −24.374 29.519 −5.829 1.00 1.00 C ATOM 4712 CD GLU A 1271 −24.500 30.969 −5.382 1.00 1.00 C ATOM 4713 OE1 GLU A 1271 −23.748 31.432 −4.489 1.00 1.00 O ATOM 4714 OE2 GLU A 1271 −25.377 31.706 −5.866 1.00 1.00 O ATOM 4715 HA GLU A 1271 −21.391 28.822 −4.345 1.00 1.00 H ATOM 4716 HB1 GLU A 1271 −22.931 28.302 −6.614 1.00 1.00 H ATOM 4717 HB2 GLU A 1271 −22.353 29.882 −6.162 1.00 1.00 H ATOM 4718 HG1 GLU A 1271 −24.752 29.499 −6.897 1.00 1.00 H ATOM 4719 HG2 GLU A 1271 −25.039 28.861 −5.281 1.00 1.00 H ATOM 4720 HN GLU A 1271 −22.287 26.431 −5.283 1.00 1.00 H ATOM 4721 N CYS A 1272 −24.377 28.177 −2.953 1.00 1.00 N ATOM 4722 CA CYS A 1272 −25.028 28.618 −1.728 1.00 1.00 C ATOM 4723 C CYS A 1272 −24.019 28.778 −0.634 1.00 1.00 C ATOM 4724 O CYS A 1272 −23.905 29.881 −0.068 1.00 1.00 O ATOM 4725 CB CYS A 1272 −26.287 27.868 −1.090 1.00 1.00 C ATOM 4726 SG CYS A 1272 −26.038 26.266 −0.273 1.00 1.00 S ATOM 4727 HA CYS A 1272 −25.479 29.580 −1.983 1.00 1.00 H ATOM 4728 HB1 CYS A 1272 −27.037 27.708 −1.889 1.00 1.00 H ATOM 4729 HB2 CYS A 1272 −26.851 28.515 −0.364 1.00 1.00 H ATOM 4730 HN CYS A 1272 −24.742 27.449 −3.500 1.00 1.00 H ATOM 4731 N PHE A 1273 −23.218 27.701 −0.319 1.00 1.00 N ATOM 4732 CA PHE A 1273 −22.126 27.837 0.652 1.00 1.00 C ATOM 4733 C PHE A 1273 −21.307 29.088 0.340 1.00 1.00 C ATOM 4734 O PHE A 1273 −21.192 29.971 1.188 1.00 1.00 O ATOM 4735 CB PHE A 1273 −21.253 26.564 0.608 1.00 1.00 C ATOM 4736 CG PHE A 1273 −19.840 26.746 1.152 1.00 1.00 C ATOM 4737 CD1 PHE A 1273 −19.619 27.238 2.433 1.00 1.00 C ATOM 4738 CD2 PHE A 1273 −18.685 26.442 0.409 1.00 1.00 C ATOM 4739 CE1 PHE A 1273 −18.356 27.482 2.917 1.00 1.00 C ATOM 4740 CE2 PHE A 1273 −17.392 26.603 0.952 1.00 1.00 C ATOM 4741 CZ PHE A 1273 −17.228 27.227 2.183 1.00 1.00 C ATOM 4742 HA PHE A 1273 −22.454 28.073 1.656 1.00 1.00 H ATOM 4743 HB1 PHE A 1273 −21.021 26.253 −0.433 1.00 1.00 H ATOM 4744 HB2 PHE A 1273 −21.839 25.724 1.065 1.00 1.00 H ATOM 4745 HD2 PHE A 1273 −18.776 26.146 −0.609 1.00 1.00 H ATOM 4746 HE2 PHE A 1273 −16.550 26.261 0.441 1.00 1.00 H ATOM 4747 HZ PHE A 1273 −16.332 27.509 2.645 1.00 1.00 H ATOM 4748 HE1 PHE A 1273 −18.212 27.892 3.911 1.00 1.00 H ATOM 4749 HD1 PHE A 1273 −20.413 27.389 3.153 1.00 1.00 H ATOM 4750 HN PHE A 1273 −23.401 26.877 −0.828 1.00 1.00 H ATOM 4751 N ARG A 1274 −20.694 29.098 −0.853 1.00 1.00 N ATOM 4752 CA ARG A 1274 −19.579 30.021 −0.925 1.00 1.00 C ATOM 4753 C ARG A 1274 −20.163 31.425 −0.719 1.00 1.00 C ATOM 4754 O ARG A 1274 −19.492 32.211 −0.080 1.00 1.00 O ATOM 4755 CB ARG A 1274 −18.682 29.902 −2.184 1.00 1.00 C ATOM 4756 CG ARG A 1274 −17.410 30.836 −2.132 1.00 1.00 C ATOM 4757 CD ARG A 1274 −16.402 30.500 −0.986 1.00 1.00 C ATOM 4758 NE ARG A 1274 −15.137 31.089 −1.376 1.00 1.00 N ATOM 4759 CZ ARG A 1274 −13.912 30.624 −1.146 1.00 1.00 C ATOM 4760 NH1 ARG A 1274 −13.583 29.569 −0.395 1.00 1.00 N ATOM 4761 NH2 ARG A 1274 −12.938 31.256 −1.722 1.00 1.00 N ATOM 4762 HA ARG A 1274 −18.858 29.846 −0.105 1.00 1.00 H ATOM 4763 HB1 ARG A 1274 −19.333 30.210 −2.995 1.00 1.00 H ATOM 4764 HB2 ARG A 1274 −18.353 28.852 −2.354 1.00 1.00 H ATOM 4765 HG1 ARG A 1274 −17.689 31.915 −2.089 1.00 1.00 H ATOM 4766 HG2 ARG A 1274 −16.919 30.664 −3.134 1.00 1.00 H ATOM 4767 HD1 ARG A 1274 −16.351 29.381 −1.000 1.00 1.00 H ATOM 4768 HD2 ARG A 1274 −16.685 30.950 0.001 1.00 1.00 H ATOM 4769 HE ARG A 1274 −15.196 31.983 −1.860 1.00 1.00 H ATOM 4770 HH12 ARG A 1274 −12.634 29.263 −0.260 1.00 1.00 H ATOM 4771 HH11 ARG A 1274 −14.328 28.981 −0.018 1.00 1.00 H ATOM 4772 HH22 ARG A 1274 −12.016 30.905 −1.563 1.00 1.00 H ATOM 4773 HH21 ARG A 1274 −13.043 32.123 −2.304 1.00 1.00 H ATOM 4774 HN ARG A 1274 −20.789 28.397 −1.533 1.00 1.00 H ATOM 4775 N LYS A 1275 −21.373 31.708 −1.231 1.00 1.00 N ATOM 4776 CA LYS A 1275 −21.857 33.144 −1.277 1.00 1.00 C ATOM 4777 C LYS A 1275 −22.813 33.412 −0.131 1.00 1.00 C ATOM 4778 O LYS A 1275 −23.423 34.485 −0.106 1.00 1.00 O ATOM 4779 CB LYS A 1275 −22.345 33.517 −2.687 1.00 1.00 C ATOM 4780 CG LYS A 1275 −22.401 35.015 −3.034 1.00 1.00 C ATOM 4781 CD LYS A 1275 −23.367 35.262 −4.262 1.00 1.00 C ATOM 4782 CE LYS A 1275 −22.855 34.715 −5.616 1.00 1.00 C ATOM 4783 NZ LYS A 1275 −23.375 33.350 −5.857 1.00 1.00 N ATOM 4784 HA LYS A 1275 −21.030 33.833 −1.205 1.00 1.00 H ATOM 4785 HB1 LYS A 1275 −23.300 33.033 −2.796 1.00 1.00 H ATOM 4786 HB2 LYS A 1275 −21.716 33.097 −3.464 1.00 1.00 H ATOM 4787 HG1 LYS A 1275 −21.440 35.406 −3.271 1.00 1.00 H ATOM 4788 HG2 LYS A 1275 −22.870 35.619 −2.241 1.00 1.00 H ATOM 4789 HD1 LYS A 1275 −23.440 36.378 −4.380 1.00 1.00 H ATOM 4790 HD2 LYS A 1275 −24.400 34.928 −4.074 1.00 1.00 H ATOM 4791 HE1 LYS A 1275 −21.753 34.731 −5.653 1.00 1.00 H ATOM 4792 HE2 LYS A 1275 −23.224 35.452 −6.394 1.00 1.00 H ATOM 4793 HZ1 LYS A 1275 −24.403 33.206 −5.742 1.00 1.00 H ATOM 4794 HZ2 LYS A 1275 −22.887 32.634 −5.250 1.00 1.00 H ATOM 4795 HZ3 LYS A 1275 −23.085 33.074 −6.889 1.00 1.00 H ATOM 4796 HN LYS A 1275 −22.017 31.066 −1.644 1.00 1.00 H ATOM 4797 N LEU A 1276 −23.067 32.472 0.832 1.00 1.00 N ATOM 4798 CA LEU A 1276 −24.034 32.794 1.881 1.00 1.00 C ATOM 4799 C LEU A 1276 −23.840 34.182 2.478 1.00 1.00 C ATOM 4800 O LEU A 1276 −24.836 34.803 2.705 1.00 1.00 O ATOM 4801 CB LEU A 1276 −24.072 31.704 3.046 1.00 1.00 C ATOM 4802 CG LEU A 1276 −25.471 31.180 3.431 1.00 1.00 C ATOM 4803 CD1 LEU A 1276 −26.311 32.295 4.042 1.00 1.00 C ATOM 4804 CD2 LEU A 1276 −26.275 30.318 2.425 1.00 1.00 C ATOM 4805 HA LEU A 1276 −25.010 32.685 1.410 1.00 1.00 H ATOM 4806 HB1 LEU A 1276 −23.521 30.832 2.725 1.00 1.00 H ATOM 4807 HB2 LEU A 1276 −23.478 32.043 3.905 1.00 1.00 H ATOM 4808 HG LEU A 1276 −25.269 30.442 4.225 1.00 1.00 H ATOM 4809 HD21 LEU A 1276 −26.551 30.897 1.548 1.00 1.00 H ATOM 4810 HD22 LEU A 1276 −25.663 29.476 2.133 1.00 1.00 H ATOM 4811 HD23 LEU A 1276 −27.191 29.945 2.853 1.00 1.00 H ATOM 4812 HD11 LEU A 1276 −26.667 32.997 3.275 1.00 1.00 H ATOM 4813 HD12 LEU A 1276 −27.168 31.843 4.535 1.00 1.00 H ATOM 4814 HD13 LEU A 1276 −25.722 32.832 4.797 1.00 1.00 H ATOM 4815 HN LEU A 1276 −22.672 31.534 0.763 1.00 1.00 H ATOM 4816 N PRO A 1277 −22.620 34.703 2.794 1.00 1.00 N ATOM 4817 CA PRO A 1277 −22.479 35.984 3.442 1.00 1.00 C ATOM 4818 C PRO A 1277 −22.884 36.048 4.922 1.00 1.00 C ATOM 4819 O PRO A 1277 −23.209 37.099 5.413 1.00 1.00 O ATOM 4820 CB PRO A 1277 −20.923 36.184 3.310 1.00 1.00 C ATOM 4821 CG PRO A 1277 −20.345 34.757 3.209 1.00 1.00 C ATOM 4822 CD PRO A 1277 −21.418 33.956 2.494 1.00 1.00 C ATOM 4823 HA PRO A 1277 −22.953 36.812 2.941 1.00 1.00 H ATOM 4824 HD2 PRO A 1277 −21.494 32.912 2.770 1.00 1.00 H ATOM 4825 HD1 PRO A 1277 −21.124 34.112 1.465 1.00 1.00 H ATOM 4826 HG2 PRO A 1277 −20.242 34.391 4.261 1.00 1.00 H ATOM 4827 HG1 PRO A 1277 −19.359 34.682 2.736 1.00 1.00 H ATOM 4828 HB1 PRO A 1277 −20.663 36.739 2.400 1.00 1.00 H ATOM 4829 HB2 PRO A 1277 −20.556 36.732 4.196 1.00 1.00 H ATOM 4830 N VAL A 1278 −22.690 34.915 5.699 1.00 1.00 N ATOM 4831 CA VAL A 1278 −23.044 34.901 7.103 1.00 1.00 C ATOM 4832 C VAL A 1278 −24.554 34.810 7.284 1.00 1.00 C ATOM 4833 O VAL A 1278 −25.044 33.788 7.744 1.00 1.00 O ATOM 4834 CB VAL A 1278 −22.242 35.880 7.989 1.00 1.00 C ATOM 4835 CG1 VAL A 1278 −22.677 35.726 9.498 1.00 1.00 C ATOM 4836 CG2 VAL A 1278 −20.730 35.639 7.776 1.00 1.00 C ATOM 4837 HA VAL A 1278 −22.687 33.976 7.450 1.00 1.00 H ATOM 4838 HB VAL A 1278 −22.491 36.871 7.671 1.00 1.00 H ATOM 4839 HG11 VAL A 1278 −22.474 34.687 9.924 1.00 1.00 H ATOM 4840 HG12 VAL A 1278 −22.248 36.541 10.174 1.00 1.00 H ATOM 4841 HG13 VAL A 1278 −23.823 35.700 9.597 1.00 1.00 H ATOM 4842 HG21 VAL A 1278 −20.446 34.672 8.184 1.00 1.00 H ATOM 4843 HG22 VAL A 1278 −20.516 35.658 6.691 1.00 1.00 H ATOM 4844 HG23 VAL A 1278 −20.122 36.459 8.179 1.00 1.00 H ATOM 4845 HN VAL A 1278 −22.438 34.017 5.306 1.00 1.00 H ATOM 4846 N ASN A 1279 −25.220 35.925 6.932 1.00 1.00 N ATOM 4847 CA ASN A 1279 −26.686 35.935 6.993 1.00 1.00 C ATOM 4848 C ASN A 1279 −27.224 35.800 8.423 1.00 1.00 C ATOM 4849 O ASN A 1279 −27.783 36.760 8.868 1.00 1.00 O ATOM 4850 CB ASN A 1279 −27.343 34.900 6.086 1.00 1.00 C ATOM 4851 CG ASN A 1279 −28.812 35.143 6.189 1.00 1.00 C ATOM 4852 OD1 ASN A 1279 −29.348 36.154 5.752 1.00 1.00 O ATOM 4853 ND2 ASN A 1279 −29.582 34.219 6.717 1.00 1.00 N ATOM 4854 HA ASN A 1279 −26.933 36.968 6.736 1.00 1.00 H ATOM 4855 HB1 ASN A 1279 −27.081 35.007 5.001 1.00 1.00 H ATOM 4856 HB2 ASN A 1279 −27.014 33.909 6.372 1.00 1.00 H ATOM 4857 HD22 ASN A 1279 −29.182 33.457 7.260 1.00 1.00 H ATOM 4858 HD21 ASN A 1279 −30.512 34.488 6.813 1.00 1.00 H ATOM 4859 HN ASN A 1279 −24.791 36.746 6.529 1.00 1.00 H ATOM 4860 N ARG A 1280 −26.981 34.700 9.150 1.00 1.00 N ATOM 4861 CA ARG A 1280 −27.561 34.508 10.472 1.00 1.00 C ATOM 4862 C ARG A 1280 −26.852 35.337 11.541 1.00 1.00 C ATOM 4863 O ARG A 1280 −26.796 36.531 11.341 1.00 1.00 O ATOM 4864 CB ARG A 1280 −29.132 34.758 10.506 1.00 1.00 C ATOM 4865 CG ARG A 1280 −29.881 34.295 11.779 1.00 1.00 C ATOM 4866 CD ARG A 1280 −31.027 33.296 11.485 1.00 1.00 C ATOM 4867 NE ARG A 1280 −30.568 32.038 10.855 1.00 1.00 N ATOM 4868 CZ ARG A 1280 −31.330 31.094 10.461 1.00 1.00 C ATOM 4869 NH1 ARG A 1280 −32.659 31.124 10.547 1.00 1.00 N ATOM 4870 NH2 ARG A 1280 −30.810 30.013 9.918 1.00 1.00 N ATOM 4871 HA ARG A 1280 −27.373 33.457 10.683 1.00 1.00 H ATOM 4872 HB1 ARG A 1280 −29.623 34.288 9.668 1.00 1.00 H ATOM 4873 HB2 ARG A 1280 −29.306 35.811 10.414 1.00 1.00 H ATOM 4874 HG1 ARG A 1280 −29.128 33.779 12.441 1.00 1.00 H ATOM 4875 HG2 ARG A 1280 −30.193 35.226 12.335 1.00 1.00 H ATOM 4876 HD1 ARG A 1280 −31.409 33.099 12.485 1.00 1.00 H ATOM 4877 HD2 ARG A 1280 −31.762 33.853 10.863 1.00 1.00 H ATOM 4878 HE ARG A 1280 −29.569 31.926 10.706 1.00 1.00 H ATOM 4879 HH12 ARG A 1280 −33.243 30.327 10.265 1.00 1.00 H ATOM 4880 HH11 ARG A 1280 −33.169 31.878 10.997 1.00 1.00 H ATOM 4881 HH22 ARG A 1280 −31.380 29.292 9.535 1.00 1.00 H ATOM 4882 HH21 ARG A 1280 −29.798 29.869 9.857 1.00 1.00 H ATOM 4883 HN ARG A 1280 −26.387 34.023 8.749 1.00 1.00 H ATOM 4884 N PRO A 1281 −26.232 34.822 12.622 1.00 1.00 N ATOM 4885 CA PRO A 1281 −26.173 33.406 12.934 1.00 1.00 C ATOM 4886 C PRO A 1281 −25.129 32.840 12.082 1.00 1.00 C ATOM 4887 O PRO A 1281 −24.527 33.527 11.249 1.00 1.00 O ATOM 4888 CB PRO A 1281 −25.770 33.527 14.449 1.00 1.00 C ATOM 4889 CG PRO A 1281 −24.763 34.737 14.388 1.00 1.00 C ATOM 4890 CD PRO A 1281 −25.546 35.737 13.526 1.00 1.00 C ATOM 4891 HA PRO A 1281 −27.069 32.853 12.847 1.00 1.00 H ATOM 4892 HD2 PRO A 1281 −24.912 36.493 13.042 1.00 1.00 H ATOM 4893 HD1 PRO A 1281 −26.295 36.311 14.117 1.00 1.00 H ATOM 4894 HG2 PRO A 1281 −23.853 34.527 13.890 1.00 1.00 H ATOM 4895 HG1 PRO A 1281 −24.536 35.126 15.392 1.00 1.00 H ATOM 4896 HB1 PRO A 1281 −26.669 33.840 15.024 1.00 1.00 H ATOM 4897 HB2 PRO A 1281 −25.316 32.650 14.914 1.00 1.00 H ATOM 4898 N ILE A 1282 −24.846 31.537 12.266 1.00 1.00 N ATOM 4899 CA ILE A 1282 −23.810 30.838 11.489 1.00 1.00 C ATOM 4900 C ILE A 1282 −24.490 29.970 10.437 1.00 1.00 C ATOM 4901 O ILE A 1282 −24.272 28.768 10.407 1.00 1.00 O ATOM 4902 CB ILE A 1282 −22.785 30.072 12.346 1.00 1.00 C ATOM 4903 CG1 ILE A 1282 −22.350 30.966 13.551 1.00 1.00 C ATOM 4904 CG2 ILE A 1282 −21.588 29.657 11.506 1.00 1.00 C ATOM 4905 CD1 ILE A 1282 −21.409 30.255 14.535 1.00 1.00 C ATOM 4906 HA ILE A 1282 −23.193 31.650 10.949 1.00 1.00 H ATOM 4907 HB ILE A 1282 −23.201 29.188 12.872 1.00 1.00 H ATOM 4908 HG11 ILE A 1282 −21.840 31.868 13.147 1.00 1.00 H ATOM 4909 HG12 ILE A 1282 −23.266 31.263 14.120 1.00 1.00 H ATOM 4910 HD11 ILE A 1282 −21.481 30.761 15.516 1.00 1.00 H ATOM 4911 HD12 ILE A 1282 −21.639 29.125 14.694 1.00 1.00 H ATOM 4912 HD13 ILE A 1282 −20.369 30.325 14.136 1.00 1.00 H ATOM 4913 HG21 ILE A 1282 −20.854 29.038 12.065 1.00 1.00 H ATOM 4914 HG22 ILE A 1282 −21.099 30.560 11.107 1.00 1.00 H ATOM 4915 HG23 ILE A 1282 −21.922 29.083 10.634 1.00 1.00 H ATOM 4916 HN ILE A 1282 −25.356 30.916 12.888 1.00 1.00 H ATOM 4917 N ASP A 1283 −25.353 30.588 9.630 1.00 1.00 N ATOM 4918 CA ASP A 1283 −25.942 29.814 8.537 1.00 1.00 C ATOM 4919 C ASP A 1283 −24.818 29.383 7.572 1.00 1.00 C ATOM 4920 O ASP A 1283 −24.874 28.307 7.014 1.00 1.00 O ATOM 4921 CB ASP A 1283 −27.009 30.600 7.815 1.00 1.00 C ATOM 4922 CG ASP A 1283 −28.119 31.135 8.667 1.00 1.00 C ATOM 4923 OD1 ASP A 1283 −28.398 30.693 9.815 1.00 1.00 O ATOM 4924 OD2 ASP A 1283 −28.864 32.100 8.281 1.00 1.00 O ATOM 4925 HA ASP A 1283 −26.528 28.925 8.905 1.00 1.00 H ATOM 4926 HB1 ASP A 1283 −26.524 31.439 7.337 1.00 1.00 H ATOM 4927 HB2 ASP A 1283 −27.482 29.955 7.068 1.00 1.00 H ATOM 4928 HN ASP A 1283 −25.513 31.584 9.624 1.00 1.00 H ATOM 4929 N TRP A 1284 −23.721 30.235 7.313 1.00 1.00 N ATOM 4930 CA TRP A 1284 −22.729 29.896 6.261 1.00 1.00 C ATOM 4931 C TRP A 1284 −22.305 28.439 6.340 1.00 1.00 C ATOM 4932 O TRP A 1284 −22.266 27.642 5.401 1.00 1.00 O ATOM 4933 CB TRP A 1284 −21.542 30.912 6.364 1.00 1.00 C ATOM 4934 CG TRP A 1284 −20.588 30.909 5.219 1.00 1.00 C ATOM 4935 CD1 TRP A 1284 −20.707 30.214 4.098 1.00 1.00 C ATOM 4936 CD2 TRP A 1284 −19.335 31.722 5.085 1.00 1.00 C ATOM 4937 NE1 TRP A 1284 −19.700 30.533 3.260 1.00 1.00 N ATOM 4938 CE2 TRP A 1284 −18.909 31.469 3.803 1.00 1.00 C ATOM 4939 CE3 TRP A 1284 −18.654 32.635 5.885 1.00 1.00 C ATOM 4940 CZ2 TRP A 1284 −17.832 32.143 3.264 1.00 1.00 C ATOM 4941 CZ3 TRP A 1284 −17.571 33.368 5.369 1.00 1.00 C ATOM 4942 CH2 TRP A 1284 −17.174 33.098 4.063 1.00 1.00 C ATOM 4943 HA TRP A 1284 −23.203 29.936 5.285 1.00 1.00 H ATOM 4944 HB1 TRP A 1284 −21.947 31.904 6.409 1.00 1.00 H ATOM 4945 HB2 TRP A 1284 −21.051 30.760 7.316 1.00 1.00 H ATOM 4946 HE1 TRP A 1284 −19.602 30.180 2.304 1.00 1.00 H ATOM 4947 HD1 TRP A 1284 −21.451 29.468 3.810 1.00 1.00 H ATOM 4948 HZ2 TRP A 1284 −17.493 31.990 2.220 1.00 1.00 H ATOM 4949 HH2 TRP A 1284 −16.255 33.610 3.689 1.00 1.00 H ATOM 4950 HZ3 TRP A 1284 −17.109 34.134 6.001 1.00 1.00 H ATOM 4951 HE3 TRP A 1284 −18.998 32.828 6.925 1.00 1.00 H ATOM 4952 HN TRP A 1284 −23.697 31.162 7.700 1.00 1.00 H ATOM 4953 N LYS A 1285 −21.955 28.062 7.583 1.00 1.00 N ATOM 4954 CA LYS A 1285 −21.533 26.684 7.777 1.00 1.00 C ATOM 4955 C LYS A 1285 −22.606 25.619 7.405 1.00 1.00 C ATOM 4956 O LYS A 1285 −22.306 24.502 6.951 1.00 1.00 O ATOM 4957 CB LYS A 1285 −20.969 26.405 9.189 1.00 1.00 C ATOM 4958 CG LYS A 1285 −20.067 25.134 9.175 1.00 1.00 C ATOM 4959 CD LYS A 1285 −19.300 24.988 10.546 1.00 1.00 C ATOM 4960 CE LYS A 1285 −20.286 24.902 11.734 1.00 1.00 C ATOM 4961 NZ LYS A 1285 −19.555 24.619 13.019 1.00 1.00 N ATOM 4962 HA LYS A 1285 −20.715 26.518 7.090 1.00 1.00 H ATOM 4963 HB1 LYS A 1285 −20.315 27.235 9.562 1.00 1.00 H ATOM 4964 HB2 LYS A 1285 −21.813 26.314 9.860 1.00 1.00 H ATOM 4965 HG1 LYS A 1285 −20.758 24.307 8.949 1.00 1.00 H ATOM 4966 HG2 LYS A 1285 −19.312 25.149 8.374 1.00 1.00 H ATOM 4967 HD1 LYS A 1285 −18.622 24.104 10.463 1.00 1.00 H ATOM 4968 HD2 LYS A 1285 −18.680 25.857 10.708 1.00 1.00 H ATOM 4969 HE1 LYS A 1285 −20.908 25.852 11.809 1.00 1.00 H ATOM 4970 HE2 LYS A 1285 −21.049 24.174 11.540 1.00 1.00 H ATOM 4971 HZ1 LYS A 1285 −18.986 23.682 12.997 1.00 1.00 H ATOM 4972 HZ2 LYS A 1285 −18.904 25.452 13.305 1.00 1.00 H ATOM 4973 HZ3 LYS A 1285 −20.145 24.672 13.932 1.00 1.00 H ATOM 4974 HN LYS A 1285 −21.920 28.704 8.393 1.00 1.00 H ATOM 4975 N VAL A 1286 −23.912 25.892 7.722 1.00 1.00 N ATOM 4976 CA VAL A 1286 −24.941 24.887 7.381 1.00 1.00 C ATOM 4977 C VAL A 1286 −25.000 24.666 5.909 1.00 1.00 C ATOM 4978 O VAL A 1286 −25.057 23.503 5.535 1.00 1.00 O ATOM 4979 CB VAL A 1286 −26.369 24.928 8.015 1.00 1.00 C ATOM 4980 CG1 VAL A 1286 −26.278 25.212 9.554 1.00 1.00 C ATOM 4981 CG2 VAL A 1286 −27.386 25.824 7.284 1.00 1.00 C ATOM 4982 HA VAL A 1286 −24.502 23.895 7.686 1.00 1.00 H ATOM 4983 HB VAL A 1286 −26.746 23.950 7.948 1.00 1.00 H ATOM 4984 HG11 VAL A 1286 −25.456 24.579 9.967 1.00 1.00 H ATOM 4985 HG12 VAL A 1286 −25.989 26.309 9.749 1.00 1.00 H ATOM 4986 HG13 VAL A 1286 −27.223 25.031 10.104 1.00 1.00 H ATOM 4987 HG21 VAL A 1286 −27.164 25.871 6.178 1.00 1.00 H ATOM 4988 HG22 VAL A 1286 −28.473 25.508 7.527 1.00 1.00 H ATOM 4989 HG23 VAL A 1286 −27.244 26.850 7.667 1.00 1.00 H ATOM 4990 HN VAL A 1286 −24.200 26.780 8.013 1.00 1.00 H ATOM 4991 N CYS A 1287 −24.882 25.584 4.956 1.00 1.00 N ATOM 4992 CA CYS A 1287 −24.666 25.224 3.534 1.00 1.00 C ATOM 4993 C CYS A 1287 −23.279 24.651 3.394 1.00 1.00 C ATOM 4994 O CYS A 1287 −23.189 23.646 2.732 1.00 1.00 O ATOM 4995 CB CYS A 1287 −24.803 26.428 2.546 1.00 1.00 C ATOM 4996 SG CYS A 1287 −26.401 26.576 1.679 1.00 1.00 S ATOM 4997 HA CYS A 1287 −25.421 24.464 3.303 1.00 1.00 H ATOM 4998 HB1 CYS A 1287 −24.506 27.401 3.066 1.00 1.00 H ATOM 4999 HB2 CYS A 1287 −24.092 26.152 1.726 1.00 1.00 H ATOM 5000 HN CYS A 1287 −24.787 26.558 5.209 1.00 1.00 H ATOM 5001 N GLN A 1288 −22.199 25.190 4.040 1.00 1.00 N ATOM 5002 CA GLN A 1288 −20.889 24.505 3.872 1.00 1.00 C ATOM 5003 C GLN A 1288 −20.953 22.968 4.034 1.00 1.00 C ATOM 5004 O GLN A 1288 −20.626 22.242 3.088 1.00 1.00 O ATOM 5005 CB GLN A 1288 −19.833 25.009 4.912 1.00 1.00 C ATOM 5006 CG GLN A 1288 −18.351 24.690 4.566 1.00 1.00 C ATOM 5007 CD GLN A 1288 −17.440 25.303 5.596 1.00 1.00 C ATOM 5008 OE1 GLN A 1288 −17.929 26.122 6.376 1.00 1.00 O ATOM 5009 NE2 GLN A 1288 −16.173 24.837 5.587 1.00 1.00 N ATOM 5010 HA GLN A 1288 −20.377 24.727 2.887 1.00 1.00 H ATOM 5011 HB1 GLN A 1288 −19.997 24.573 5.928 1.00 1.00 H ATOM 5012 HB2 GLN A 1288 −20.005 26.076 5.038 1.00 1.00 H ATOM 5013 HG1 GLN A 1288 −18.289 23.625 4.533 1.00 1.00 H ATOM 5014 HG2 GLN A 1288 −18.085 24.965 3.553 1.00 1.00 H ATOM 5015 HE22 GLN A 1288 −15.502 25.206 6.238 1.00 1.00 H ATOM 5016 HE21 GLN A 1288 −15.880 24.085 5.031 1.00 1.00 H ATOM 5017 HN GLN A 1288 −22.281 25.997 4.567 1.00 1.00 H ATOM 5018 N ARG A 1289 −21.392 22.473 5.191 1.00 1.00 N ATOM 5019 CA ARG A 1289 −21.449 20.979 5.448 1.00 1.00 C ATOM 5020 C ARG A 1289 −22.850 20.434 5.293 1.00 1.00 C ATOM 5021 O ARG A 1289 −22.838 19.206 5.337 1.00 1.00 O ATOM 5022 CB ARG A 1289 −20.782 20.562 6.807 1.00 1.00 C ATOM 5023 CG ARG A 1289 −19.343 21.192 6.988 1.00 1.00 C ATOM 5024 CD ARG A 1289 −18.291 21.005 5.872 1.00 1.00 C ATOM 5025 NE ARG A 1289 −17.962 19.617 5.478 1.00 1.00 N ATOM 5026 CZ ARG A 1289 −17.211 19.325 4.416 1.00 1.00 C ATOM 5027 NH1 ARG A 1289 −16.627 20.215 3.647 1.00 1.00 N ATOM 5028 NH2 ARG A 1289 −17.063 18.063 4.155 1.00 1.00 N ATOM 5029 HA ARG A 1289 −20.833 20.443 4.754 1.00 1.00 H ATOM 5030 HB1 ARG A 1289 −20.739 19.454 7.023 1.00 1.00 H ATOM 5031 HB2 ARG A 1289 −21.432 20.968 7.605 1.00 1.00 H ATOM 5032 HG1 ARG A 1289 −19.443 22.232 7.281 1.00 1.00 H ATOM 5033 HG2 ARG A 1289 −18.833 20.651 7.843 1.00 1.00 H ATOM 5034 HD1 ARG A 1289 −18.739 21.477 4.956 1.00 1.00 H ATOM 5035 HD2 ARG A 1289 −17.316 21.491 6.091 1.00 1.00 H ATOM 5036 HE ARG A 1289 −18.447 18.851 5.946 1.00 1.00 H ATOM 5037 HH12 ARG A 1289 −16.147 19.911 2.804 1.00 1.00 H ATOM 5038 HH11 ARG A 1289 −16.723 21.211 3.837 1.00 1.00 H ATOM 5039 HH22 ARG A 1289 −16.578 17.777 3.316 1.00 1.00 H ATOM 5040 HH21 ARG A 1289 −17.446 17.328 4.682 1.00 1.00 H ATOM 5041 HN ARG A 1289 −21.746 23.047 5.935 1.00 1.00 H ATOM 5042 N ILE A 1290 −24.029 21.104 5.065 1.00 1.00 N ATOM 5043 CA ILE A 1290 −25.199 20.409 4.492 1.00 1.00 C ATOM 5044 C ILE A 1290 −24.738 20.093 3.114 1.00 1.00 C ATOM 5045 O ILE A 1290 −24.827 18.945 2.738 1.00 1.00 O ATOM 5046 CB ILE A 1290 −26.564 21.164 4.445 1.00 1.00 C ATOM 5047 CG1 ILE A 1290 −27.144 21.374 5.911 1.00 1.00 C ATOM 5048 CG2 ILE A 1290 −27.589 20.357 3.587 1.00 1.00 C ATOM 5049 CD1 ILE A 1290 −28.258 22.462 5.926 1.00 1.00 C ATOM 5050 HA ILE A 1290 −25.348 19.470 5.101 1.00 1.00 H ATOM 5051 HB ILE A 1290 −26.421 22.203 3.996 1.00 1.00 H ATOM 5052 HG11 ILE A 1290 −27.587 20.432 6.327 1.00 1.00 H ATOM 5053 HG12 ILE A 1290 −26.308 21.737 6.585 1.00 1.00 H ATOM 5054 HD11 ILE A 1290 −28.641 22.447 6.939 1.00 1.00 H ATOM 5055 HD12 ILE A 1290 −29.036 22.304 5.151 1.00 1.00 H ATOM 5056 HD13 ILE A 1290 −27.946 23.491 5.755 1.00 1.00 H ATOM 5057 HG21 ILE A 1290 −27.167 19.995 2.670 1.00 1.00 H ATOM 5058 HG22 ILE A 1290 −28.480 20.948 3.393 1.00 1.00 H ATOM 5059 HG23 ILE A 1290 −27.894 19.413 4.137 1.00 1.00 H ATOM 5060 HN ILE A 1290 −24.124 22.088 5.229 1.00 1.00 H ATOM 5061 N VAL A 1291 −24.239 21.031 2.334 1.00 1.00 N ATOM 5062 CA VAL A 1291 −23.758 20.681 0.964 1.00 1.00 C ATOM 5063 C VAL A 1291 −22.719 19.577 1.056 1.00 1.00 C ATOM 5064 O VAL A 1291 −22.837 18.617 0.321 1.00 1.00 O ATOM 5065 CB VAL A 1291 −23.121 21.836 0.148 1.00 1.00 C ATOM 5066 CG1 VAL A 1291 −22.367 21.316 −1.151 1.00 1.00 C ATOM 5067 CG2 VAL A 1291 −24.145 22.950 −0.186 1.00 1.00 C ATOM 5068 HA VAL A 1291 −24.658 20.317 0.330 1.00 1.00 H ATOM 5069 HB VAL A 1291 −22.349 22.272 0.752 1.00 1.00 H ATOM 5070 HG11 VAL A 1291 −21.924 22.095 −1.786 1.00 1.00 H ATOM 5071 HG12 VAL A 1291 −21.578 20.572 −0.957 1.00 1.00 H ATOM 5072 HG13 VAL A 1291 −23.140 20.784 −1.738 1.00 1.00 H ATOM 5073 HG21 VAL A 1291 −24.961 22.541 −0.786 1.00 1.00 H ATOM 5074 HG22 VAL A 1291 −24.553 23.343 0.731 1.00 1.00 H ATOM 5075 HG23 VAL A 1291 −23.695 23.764 −0.752 1.00 1.00 H ATOM 5076 HN VAL A 1291 −24.072 21.937 2.683 1.00 1.00 H ATOM 5077 N GLY A 1292 −21.680 19.743 1.925 1.00 1.00 N ATOM 5078 CA GLY A 1292 −20.756 18.618 2.128 1.00 1.00 C ATOM 5079 C GLY A 1292 −21.518 17.368 2.405 1.00 1.00 C ATOM 5080 O GLY A 1292 −21.404 16.429 1.654 1.00 1.00 O ATOM 5081 HA2 GLY A 1292 −20.090 18.886 2.900 1.00 1.00 H ATOM 5082 HA1 GLY A 1292 −20.189 18.685 1.202 1.00 1.00 H ATOM 5083 HN GLY A 1292 −21.547 20.589 2.495 1.00 1.00 H ATOM 5084 N LEU A 1293 −22.288 17.318 3.509 1.00 1.00 N ATOM 5085 CA LEU A 1293 −22.853 16.043 3.938 1.00 1.00 C ATOM 5086 C LEU A 1293 −23.660 15.500 2.777 1.00 1.00 C ATOM 5087 O LEU A 1293 −23.602 14.291 2.562 1.00 1.00 O ATOM 5088 CB LEU A 1293 −23.786 16.313 5.181 1.00 1.00 C ATOM 5089 CG LEU A 1293 −24.323 14.954 5.735 1.00 1.00 C ATOM 5090 CD1 LEU A 1293 −23.229 13.957 6.249 1.00 1.00 C ATOM 5091 CD2 LEU A 1293 −25.425 15.232 6.797 1.00 1.00 C ATOM 5092 HA LEU A 1293 −22.039 15.362 4.191 1.00 1.00 H ATOM 5093 HB1 LEU A 1293 −24.578 16.981 4.837 1.00 1.00 H ATOM 5094 HB2 LEU A 1293 −23.295 16.857 5.993 1.00 1.00 H ATOM 5095 HG LEU A 1293 −24.926 14.462 4.932 1.00 1.00 H ATOM 5096 HD21 LEU A 1293 −25.898 14.249 7.026 1.00 1.00 H ATOM 5097 HD22 LEU A 1293 −24.960 15.651 7.725 1.00 1.00 H ATOM 5098 HD23 LEU A 1293 −26.201 15.951 6.435 1.00 1.00 H ATOM 5099 HD11 LEU A 1293 −22.687 13.486 5.449 1.00 1.00 H ATOM 5100 HD12 LEU A 1293 −22.495 14.505 6.842 1.00 1.00 H ATOM 5101 HD13 LEU A 1293 −23.727 13.212 6.853 1.00 1.00 H ATOM 5102 HN LEU A 1293 −22.372 18.140 4.079 1.00 1.00 H ATOM 5103 N LEU A 1294 −24.387 16.328 1.962 1.00 1.00 N ATOM 5104 CA LEU A 1294 −25.163 15.668 0.916 1.00 1.00 C ATOM 5105 C LEU A 1294 −24.195 14.975 −0.083 1.00 1.00 C ATOM 5106 O LEU A 1294 −24.331 13.816 −0.397 1.00 1.00 O ATOM 5107 CB LEU A 1294 −26.218 16.551 0.156 1.00 1.00 C ATOM 5108 CG LEU A 1294 −27.019 15.788 −0.933 1.00 1.00 C ATOM 5109 CD1 LEU A 1294 −28.049 14.762 −0.438 1.00 1.00 C ATOM 5110 CD2 LEU A 1294 −27.829 16.828 −1.784 1.00 1.00 C ATOM 5111 HA LEU A 1294 −25.828 14.912 1.343 1.00 1.00 H ATOM 5112 HB1 LEU A 1294 −25.616 17.340 −0.349 1.00 1.00 H ATOM 5113 HB2 LEU A 1294 −26.942 17.032 0.829 1.00 1.00 H ATOM 5114 HG LEU A 1294 −26.377 15.136 −1.568 1.00 1.00 H ATOM 5115 HD21 LEU A 1294 −28.414 16.337 −2.587 1.00 1.00 H ATOM 5116 HD22 LEU A 1294 −28.587 17.436 −1.216 1.00 1.00 H ATOM 5117 HD23 LEU A 1294 −27.113 17.569 −2.229 1.00 1.00 H ATOM 5118 HD11 LEU A 1294 −28.664 15.362 0.202 1.00 1.00 H ATOM 5119 HD12 LEU A 1294 −28.591 14.307 −1.290 1.00 1.00 H ATOM 5120 HD13 LEU A 1294 −27.589 13.884 0.100 1.00 1.00 H ATOM 5121 HN LEU A 1294 −24.496 17.321 2.088 1.00 1.00 H ATOM 5122 N GLY A 1295 −23.225 15.729 −0.655 1.00 1.00 N ATOM 5123 CA GLY A 1295 −22.317 15.047 −1.600 1.00 1.00 C ATOM 5124 C GLY A 1295 −21.521 13.872 −0.969 1.00 1.00 C ATOM 5125 O GLY A 1295 −21.392 12.842 −1.610 1.00 1.00 O ATOM 5126 HA2 GLY A 1295 −21.531 15.810 −1.917 1.00 1.00 H ATOM 5127 HA1 GLY A 1295 −22.772 14.705 −2.529 1.00 1.00 H ATOM 5128 HN GLY A 1295 −23.065 16.709 −0.403 1.00 1.00 H ATOM 5129 N PHE A 1296 −21.035 14.020 0.272 1.00 1.00 N ATOM 5130 CA PHE A 1296 −20.367 12.901 0.937 1.00 1.00 C ATOM 5131 C PHE A 1296 −21.308 11.818 1.459 1.00 1.00 C ATOM 5132 O PHE A 1296 −20.882 10.686 1.508 1.00 1.00 O ATOM 5133 CB PHE A 1296 −19.471 13.486 2.037 1.00 1.00 C ATOM 5134 CG PHE A 1296 −18.879 12.326 2.879 1.00 1.00 C ATOM 5135 CD1 PHE A 1296 −17.816 11.596 2.337 1.00 1.00 C ATOM 5136 CD2 PHE A 1296 −19.393 12.034 4.151 1.00 1.00 C ATOM 5137 CE1 PHE A 1296 −17.387 10.456 2.964 1.00 1.00 C ATOM 5138 CE2 PHE A 1296 −18.809 10.971 4.840 1.00 1.00 C ATOM 5139 CZ PHE A 1296 −17.851 10.152 4.254 1.00 1.00 C ATOM 5140 HA PHE A 1296 −19.732 12.341 0.210 1.00 1.00 H ATOM 5141 HB1 PHE A 1296 −20.116 14.119 2.688 1.00 1.00 H ATOM 5142 HB2 PHE A 1296 −18.763 14.124 1.499 1.00 1.00 H ATOM 5143 HD2 PHE A 1296 −20.206 12.582 4.623 1.00 1.00 H ATOM 5144 HE2 PHE A 1296 −19.057 10.723 5.856 1.00 1.00 H ATOM 5145 HZ PHE A 1296 −17.494 9.302 4.804 1.00 1.00 H ATOM 5146 HE1 PHE A 1296 −16.664 9.862 2.404 1.00 1.00 H ATOM 5147 HD1 PHE A 1296 −17.317 11.922 1.440 1.00 1.00 H ATOM 5148 HN PHE A 1296 −21.241 14.818 0.840 1.00 1.00 H ATOM 5149 N ALA A 1297 −22.562 12.097 1.878 1.00 1.00 N ATOM 5150 CA ALA A 1297 −23.413 11.025 2.368 1.00 1.00 C ATOM 5151 C ALA A 1297 −24.054 10.314 1.244 1.00 1.00 C ATOM 5152 O ALA A 1297 −24.071 9.085 1.299 1.00 1.00 O ATOM 5153 CB ALA A 1297 −24.579 11.506 3.256 1.00 1.00 C ATOM 5154 HA ALA A 1297 −22.846 10.374 3.041 1.00 1.00 H ATOM 5155 HB1 ALA A 1297 −25.266 10.703 3.651 1.00 1.00 H ATOM 5156 HB2 ALA A 1297 −24.142 12.032 4.124 1.00 1.00 H ATOM 5157 HB3 ALA A 1297 −25.086 12.269 2.636 1.00 1.00 H ATOM 5158 HN ALA A 1297 −22.910 13.051 1.858 1.00 1.00 H ATOM 5159 N ALA A 1298 −24.555 10.972 0.170 1.00 1.00 N ATOM 5160 CA ALA A 1298 −25.210 10.256 −0.945 1.00 1.00 C ATOM 5161 C ALA A 1298 −24.470 8.996 −1.349 1.00 1.00 C ATOM 5162 O ALA A 1298 −25.143 7.965 −1.331 1.00 1.00 O ATOM 5163 CB ALA A 1298 −25.423 11.143 −2.207 1.00 1.00 C ATOM 5164 HA ALA A 1298 −26.212 9.912 −0.647 1.00 1.00 H ATOM 5165 HB1 ALA A 1298 −25.717 10.662 −3.116 1.00 1.00 H ATOM 5166 HB2 ALA A 1298 −26.154 11.910 −1.990 1.00 1.00 H ATOM 5167 HB3 ALA A 1298 −24.536 11.685 −2.406 1.00 1.00 H ATOM 5168 HN ALA A 1298 −24.448 11.946 0.093 1.00 1.00 H ATOM 5169 N PRO A 1299 −23.165 8.930 −1.686 1.00 1.00 N ATOM 5170 CA PRO A 1299 −22.610 7.606 −1.942 1.00 1.00 C ATOM 5171 C PRO A 1299 −22.766 6.828 −0.660 1.00 1.00 C ATOM 5172 O PRO A 1299 −23.394 5.773 −0.717 1.00 1.00 O ATOM 5173 CB PRO A 1299 −21.130 8.014 −2.205 1.00 1.00 C ATOM 5174 CG PRO A 1299 −20.921 9.287 −1.426 1.00 1.00 C ATOM 5175 CD PRO A 1299 −22.266 10.052 −1.590 1.00 1.00 C ATOM 5176 HA PRO A 1299 −23.038 7.151 −2.833 1.00 1.00 H ATOM 5177 HD2 PRO A 1299 −22.467 10.718 −0.735 1.00 1.00 H ATOM 5178 HD1 PRO A 1299 −22.232 10.660 −2.522 1.00 1.00 H ATOM 5179 HG2 PRO A 1299 −20.077 9.958 −1.715 1.00 1.00 H ATOM 5180 HG1 PRO A 1299 −20.796 9.026 −0.406 1.00 1.00 H ATOM 5181 HB1 PRO A 1299 −20.955 8.397 −3.271 1.00 1.00 H ATOM 5182 HB2 PRO A 1299 −20.384 7.217 −1.913 1.00 1.00 H ATOM 5183 H31 PRO A 1299 −22.431 7.050 0.365 1.00 1.00 H TER ATOM 5184 P G B 1 9.978 18.634 9.126 1.00 1.00 P ATOM 5185 O1P G B 1 10.277 17.475 9.966 1.00 1.00 O ATOM 5186 O2P G B 1 10.102 18.062 7.766 1.00 1.00 O ATOM 5187 O5* G B 1 8.510 19.136 9.514 1.00 1.00 O ATOM 5188 C5* G B 1 8.248 19.280 10.931 1.00 1.00 C ATOM 5189 C4* G B 1 6.746 19.746 11.168 1.00 1.00 C ATOM 5190 O4* G B 1 6.518 19.998 12.557 1.00 1.00 O ATOM 5191 C1* G B 1 5.335 20.855 12.697 1.00 1.00 C ATOM 5192 C2* G B 1 5.612 21.906 11.578 1.00 1.00 C ATOM 5193 C3* G B 1 6.415 21.088 10.493 1.00 1.00 C ATOM 5194 O3* G B 1 5.718 20.964 9.265 1.00 1.00 O ATOM 5195 N9 G B 1 5.412 21.337 14.003 1.00 1.00 N ATOM 5196 C8 G B 1 5.143 22.572 14.356 1.00 1.00 C ATOM 5197 N7 G B 1 5.247 22.678 15.573 1.00 1.00 N ATOM 5198 C5 G B 1 5.683 21.440 16.154 1.00 1.00 C ATOM 5199 O6 G B 1 5.978 21.702 18.480 1.00 1.00 O ATOM 5200 C6 G B 1 6.043 20.972 17.505 1.00 1.00 C ATOM 5201 N1 G B 1 6.476 19.724 17.548 1.00 1.00 N ATOM 5202 N2 G B 1 6.914 17.651 16.668 1.00 1.00 N ATOM 5203 C2 G B 1 6.528 18.879 16.468 1.00 1.00 C ATOM 5204 N3 G B 1 6.179 19.274 15.283 1.00 1.00 N ATOM 5205 C4 G B 1 5.768 20.640 15.077 1.00 1.00 C ATOM 5206 H5*1 G B 1 8.998 20.043 11.193 1.00 1.00 H ATOM 5207 H5*2 G B 1 8.486 18.304 11.400 1.00 1.00 H ATOM 5208 H4* G B 1 6.016 18.952 10.935 1.00 1.00 H ATOM 5209 H1* G B 1 4.424 20.186 12.584 1.00 1.00 H ATOM 5210 H2*1 G B 1 4.666 22.418 11.192 1.00 1.00 H ATOM 5211 H2*2 G B 1 6.285 22.640 12.065 1.00 1.00 H ATOM 5212 H3* G B 1 7.347 21.621 10.220 1.00 1.00 H ATOM 5213 H8 G B 1 4.823 23.435 13.769 1.00 1.00 H ATOM 5214 H1 G B 1 6.878 19.425 18.396 1.00 1.00 H ATOM 5215 H21 G B 1 6.964 16.996 15.892 1.00 1.00 H ATOM 5216 H22 G B 1 7.155 17.326 17.602 1.00 1.00 H ATOM 5217 H7 G B 1 10.699 19.344 9.220 1.00 1.00 H ATOM 5218 P C B 2 4.267 20.344 9.004 1.00 1.00 P ATOM 5219 O1P C B 2 3.540 20.364 10.306 1.00 1.00 O ATOM 5220 O2P C B 2 4.527 18.955 8.532 1.00 1.00 O ATOM 5221 O5* C B 2 3.530 21.270 7.815 1.00 1.00 O ATOM 5222 C5* C B 2 3.449 20.849 6.433 1.00 1.00 C ATOM 5223 C4* C B 2 2.281 19.883 6.091 1.00 1.00 C ATOM 5224 O4* C B 2 2.138 18.943 7.135 1.00 1.00 O ATOM 5225 C1* C B 2 0.717 18.660 7.292 1.00 1.00 C ATOM 5226 C2* C B 2 0.259 20.093 7.262 1.00 1.00 C ATOM 5227 C3* C B 2 0.885 20.556 5.946 1.00 1.00 C ATOM 5228 O3* C B 2 0.194 19.995 4.783 1.00 1.00 O ATOM 5229 N1 C B 2 0.191 18.057 8.505 1.00 1.00 N ATOM 5230 C6 C B 2 1.013 17.927 9.608 1.00 1.00 C ATOM 5231 C5 C B 2 0.476 17.687 10.797 1.00 1.00 C ATOM 5232 N4 C B 2 −1.449 17.099 12.119 1.00 1.00 N ATOM 5233 C4 C B 2 −0.988 17.392 10.928 1.00 1.00 C ATOM 5234 N3 C B 2 −1.705 17.494 9.917 1.00 1.00 N ATOM 5235 O2 C B 2 −1.942 17.972 7.742 1.00 1.00 O ATOM 5236 C2 C B 2 −1.144 17.855 8.619 1.00 1.00 C ATOM 5237 H5*1 C B 2 4.388 20.292 6.198 1.00 1.00 H ATOM 5238 H5*2 C B 2 3.339 21.768 5.845 1.00 1.00 H ATOM 5239 H4* C B 2 2.440 19.341 5.153 1.00 1.00 H ATOM 5240 H1* C B 2 0.443 18.085 6.408 1.00 1.00 H ATOM 5241 H2*1 C B 2 −0.852 20.244 7.232 1.00 1.00 H ATOM 5242 H2*2 C B 2 0.620 20.576 8.166 1.00 1.00 H ATOM 5243 H3* C B 2 0.944 21.697 5.877 1.00 1.00 H ATOM 5244 H6 C B 2 2.077 18.043 9.585 1.00 1.00 H ATOM 5245 H5 C B 2 1.051 17.689 11.755 1.00 1.00 H ATOM 5246 H41 C B 2 −2.492 16.979 12.204 1.00 1.00 H ATOM 5247 H42 C B 2 −0.832 17.071 12.983 1.00 1.00 H ATOM 5248 P T B 3 0.531 20.461 3.283 1.00 1.00 P ATOM 5249 O1P T B 3 1.714 21.375 3.428 1.00 1.00 O ATOM 5250 O2P T B 3 −0.563 21.190 2.607 1.00 1.00 O ATOM 5251 O5* T B 3 0.867 19.198 2.338 1.00 1.00 O ATOM 5252 C5* T B 3 2.104 19.085 1.624 1.00 1.00 C ATOM 5253 C4* T B 3 2.230 17.859 0.722 1.00 1.00 C ATOM 5254 O4* T B 3 1.867 16.569 1.217 1.00 1.00 O ATOM 5255 C1* T B 3 1.388 15.704 0.194 1.00 1.00 C ATOM 5256 C2* T B 3 1.647 16.528 −1.104 1.00 1.00 C ATOM 5257 C3* T B 3 1.498 17.993 −0.621 1.00 1.00 C ATOM 5258 O3* T B 3 2.178 18.878 −1.514 1.00 1.00 O ATOM 5259 N1 T B 3 −0.073 15.623 0.222 1.00 1.00 N ATOM 5260 C2 T B 3 −0.638 14.661 −0.549 1.00 1.00 C ATOM 5261 N3 T B 3 −1.957 14.543 −0.598 1.00 1.00 N ATOM 5262 C4 T B 3 −2.745 15.471 0.002 1.00 1.00 C ATOM 5263 C5 T B 3 −2.177 16.579 0.805 1.00 1.00 C ATOM 5264 C6 T B 3 −0.822 16.506 0.920 1.00 1.00 C ATOM 5265 O2 T B 3 0.061 13.901 −1.193 1.00 1.00 O ATOM 5266 O4 T B 3 −3.954 15.429 −0.123 1.00 1.00 O ATOM 5267 H5*1 T B 3 2.902 19.048 2.380 1.00 1.00 H ATOM 5268 H5*2 T B 3 2.172 20.025 1.032 1.00 1.00 H ATOM 5269 H4* T B 3 3.290 17.742 0.435 1.00 1.00 H ATOM 5270 H1* T B 3 1.883 14.726 0.261 1.00 1.00 H ATOM 5271 H2*1 T B 3 2.665 16.338 −1.409 1.00 1.00 H ATOM 5272 H2*2 T B 3 0.940 16.332 −1.878 1.00 1.00 H ATOM 5273 H3* T B 3 0.444 18.369 −0.486 1.00 1.00 H ATOM 5274 C5M T B 3 −2.995 17.692 1.395 1.00 1.00 C ATOM 5275 H3 T B 3 −2.354 13.838 −1.154 1.00 1.00 H ATOM 5276 H6 T B 3 −0.396 17.254 1.605 1.00 1.00 H ATOM 5277 H51 T B 3 −2.442 18.470 1.922 1.00 1.00 H ATOM 5278 H52 T B 3 −3.470 18.142 0.549 1.00 1.00 H ATOM 5279 H53 T B 3 −3.669 17.252 2.154 1.00 1.00 H ATOM 5280 P C B 4 1.561 19.388 −2.878 1.00 1.00 P ATOM 5281 O1P C B 4 2.677 20.130 −3.600 1.00 1.00 O ATOM 5282 O2P C B 4 0.383 20.212 −2.556 1.00 1.00 O ATOM 5283 O5* C B 4 1.047 18.176 −3.736 1.00 1.00 O ATOM 5284 C5* C B 4 2.000 17.454 −4.536 1.00 1.00 C ATOM 5285 C4* C B 4 1.184 16.382 −5.282 1.00 1.00 C ATOM 5286 O4* C B 4 0.388 15.518 −4.414 1.00 1.00 O ATOM 5287 C1* C B 4 −0.688 14.937 −5.214 1.00 1.00 C ATOM 5288 C2* C B 4 −0.631 15.630 −6.572 1.00 1.00 C ATOM 5289 C3* C B 4 0.117 16.950 −6.225 1.00 1.00 C ATOM 5290 O3* C B 4 0.785 17.584 −7.342 1.00 1.00 O ATOM 5291 N1 C B 4 −1.934 15.167 −4.500 1.00 1.00 N ATOM 5292 C6 C B 4 −2.059 16.149 −3.529 1.00 1.00 C ATOM 5293 C5 C B 4 −3.193 16.353 −2.851 1.00 1.00 C ATOM 5294 N4 C B 4 −5.517 15.681 −2.416 1.00 1.00 N ATOM 5295 C4 C B 4 −4.389 15.482 −3.064 1.00 1.00 C ATOM 5296 N3 C B 4 −4.253 14.585 −3.968 1.00 1.00 N ATOM 5297 O2 C B 4 −3.029 13.620 −5.620 1.00 1.00 O ATOM 5298 C2 C B 4 −3.030 14.446 −4.755 1.00 1.00 C ATOM 5299 H5*1 C B 4 2.709 16.938 −3.850 1.00 1.00 H ATOM 5300 H5*2 C B 4 2.618 18.047 −5.232 1.00 1.00 H ATOM 5301 H4* C B 4 1.816 15.761 −5.860 1.00 1.00 H ATOM 5302 H1* C B 4 −0.404 13.904 −5.379 1.00 1.00 H ATOM 5303 H2*1 C B 4 −0.113 15.024 −7.307 1.00 1.00 H ATOM 5304 H2*2 C B 4 −1.598 15.862 −7.024 1.00 1.00 H ATOM 5305 H3* C B 4 −0.515 17.660 −5.704 1.00 1.00 H ATOM 5306 H6 C B 4 −1.232 16.784 −3.287 1.00 1.00 H ATOM 5307 H5 C B 4 −3.265 17.160 −2.124 1.00 1.00 H ATOM 5308 H41 C B 4 −6.260 15.014 −2.594 1.00 1.00 H ATOM 5309 H42 C B 4 −5.629 16.394 −1.695 1.00 1.00 H ATOM 5310 P C B 5 −0.082 18.421 −8.434 1.00 1.00 P ATOM 5311 O1P C B 5 0.753 19.086 −9.468 1.00 1.00 O ATOM 5312 O2P C B 5 −0.938 19.477 −7.812 1.00 1.00 O ATOM 5313 O5* C B 5 −1.252 17.568 −9.193 1.00 1.00 O ATOM 5314 C5* C B 5 −0.945 16.544 −10.159 1.00 1.00 C ATOM 5315 C4* C B 5 −2.253 15.860 −10.519 1.00 1.00 C ATOM 5316 O4* C B 5 −2.788 15.182 −9.353 1.00 1.00 O ATOM 5317 C1* C B 5 −4.211 15.075 −9.504 1.00 1.00 C ATOM 5318 C2* C B 5 −4.606 15.929 −10.715 1.00 1.00 C ATOM 5319 C3* C B 5 −3.400 16.849 −10.827 1.00 1.00 C ATOM 5320 O3* C B 5 −3.195 17.595 −12.046 1.00 1.00 O ATOM 5321 N1 C B 5 −4.866 15.581 −8.255 1.00 1.00 N ATOM 5322 C6 C B 5 −4.260 16.608 −7.510 1.00 1.00 C ATOM 5323 C5 C B 5 −4.745 16.993 −6.318 1.00 1.00 C ATOM 5324 N4 C B 5 −6.514 16.782 −4.720 1.00 1.00 N ATOM 5325 C4 C B 5 −5.986 16.360 −5.816 1.00 1.00 C ATOM 5326 N3 C B 5 −6.565 15.501 −6.568 1.00 1.00 N ATOM 5327 O2 C B 5 −6.532 14.166 −8.366 1.00 1.00 O ATOM 5328 C2 C B 5 −5.951 15.023 −7.758 1.00 1.00 C ATOM 5329 H5*1 C B 5 −0.240 15.825 −9.713 1.00 1.00 H ATOM 5330 H5*2 C B 5 −0.456 17.026 −11.048 1.00 1.00 H ATOM 5331 H4* C B 5 −2.112 15.168 −11.381 1.00 1.00 H ATOM 5332 H1* C B 5 −4.475 14.004 −9.663 1.00 1.00 H ATOM 5333 H2*1 C B 5 −4.669 15.306 −11.628 1.00 1.00 H ATOM 5334 H2*2 C B 5 −5.536 16.501 −10.550 1.00 1.00 H ATOM 5335 H3* C B 5 −3.591 17.543 −9.995 1.00 1.00 H ATOM 5336 H6 C B 5 −3.337 17.169 −7.851 1.00 1.00 H ATOM 5337 H5 C B 5 −4.194 17.786 −5.803 1.00 1.00 H ATOM 5338 H41 C B 5 −7.404 16.352 −4.396 1.00 1.00 H ATOM 5339 H42 C B 5 −6.101 17.579 −4.246 1.00 1.00 H ATOM 5340 P G B 6 −4.141 18.837 −12.375 1.00 1.00 P ATOM 5341 O1P G B 6 −3.892 19.366 −13.746 1.00 1.00 O ATOM 5342 O2P G B 6 −3.858 19.867 −11.325 1.00 1.00 O ATOM 5343 O5* G B 6 −5.626 18.343 −12.302 1.00 1.00 O ATOM 5344 C5* G B 6 −6.042 17.556 −13.417 1.00 1.00 C ATOM 5345 C4* G B 6 −7.460 17.098 −13.243 1.00 1.00 C ATOM 5346 O4* G B 6 −7.649 16.422 −12.004 1.00 1.00 O ATOM 5347 C1* G B 6 −9.012 16.648 −11.571 1.00 1.00 C ATOM 5348 C2* G B 6 −9.665 17.662 −12.569 1.00 1.00 C ATOM 5349 C3* G B 6 −8.399 18.287 −13.229 1.00 1.00 C ATOM 5350 O3* G B 6 −8.613 18.684 −14.589 1.00 1.00 O ATOM 5351 N9 G B 6 −9.007 17.278 −10.242 1.00 1.00 N ATOM 5352 C8 G B 6 −8.002 17.936 −9.762 1.00 1.00 C ATOM 5353 N7 G B 6 −8.243 18.346 −8.613 1.00 1.00 N ATOM 5354 C5 G B 6 −9.547 17.905 −8.229 1.00 1.00 C ATOM 5355 O6 G B 6 −10.018 18.697 −6.117 1.00 1.00 O ATOM 5356 C6 G B 6 −10.426 18.019 −7.054 1.00 1.00 C ATOM 5357 N1 G B 6 −11.585 17.363 −7.121 1.00 1.00 N ATOM 5358 N2 G B 6 −13.217 16.295 −8.350 1.00 1.00 N ATOM 5359 C2 G B 6 −12.001 16.769 −8.278 1.00 1.00 C ATOM 5360 N3 G B 6 −11.237 16.666 −9.295 1.00 1.00 N ATOM 5361 C4 G B 6 −9.901 17.258 −9.311 1.00 1.00 C ATOM 5362 H5*1 G B 6 −5.424 16.682 −13.501 1.00 1.00 H ATOM 5363 H5*2 G B 6 −5.913 18.140 −14.341 1.00 1.00 H ATOM 5364 H4* G B 6 −7.856 16.388 −13.972 1.00 1.00 H ATOM 5365 H1* G B 6 −9.590 15.714 −11.561 1.00 1.00 H ATOM 5366 H2*1 G B 6 −10.202 17.179 −13.354 1.00 1.00 H ATOM 5367 H2*2 G B 6 −10.335 18.377 −12.078 1.00 1.00 H ATOM 5368 H3* G B 6 −8.035 19.065 −12.481 1.00 1.00 H ATOM 5369 H8 G B 6 −7.050 18.175 −10.196 1.00 1.00 H ATOM 5370 H1 G B 6 −12.148 17.353 −6.308 1.00 1.00 H ATOM 5371 H21 G B 6 −13.585 15.802 −9.236 1.00 1.00 H ATOM 5372 H22 G B 6 −13.840 16.331 −7.544 1.00 1.00 H ATOM 5373 P G B 7 −9.381 20.019 −15.030 1.00 1.00 P ATOM 5374 O1P G B 7 −9.383 20.234 −16.502 1.00 1.00 O ATOM 5375 O2P G B 7 −8.636 21.113 −14.333 1.00 1.00 O ATOM 5376 O5* G B 7 −10.895 20.032 −14.650 1.00 1.00 O ATOM 5377 C5* G B 7 −11.912 19.244 −15.204 1.00 1.00 C ATOM 5378 C4* G B 7 −13.143 19.170 −14.242 1.00 1.00 C ATOM 5379 O4* G B 7 −12.862 18.629 −12.908 1.00 1.00 O ATOM 5380 C1* G B 7 −13.712 19.248 −11.948 1.00 1.00 C ATOM 5381 C2* G B 7 −14.637 20.219 −12.763 1.00 1.00 C ATOM 5382 C3* G B 7 −13.666 20.583 −13.910 1.00 1.00 C ATOM 5383 O3* G B 7 −14.394 21.039 −15.085 1.00 1.00 O ATOM 5384 N9 G B 7 −12.822 19.896 −10.989 1.00 1.00 N ATOM 5385 C8 G B 7 −11.666 20.404 −11.172 1.00 1.00 C ATOM 5386 N7 G B 7 −11.146 20.780 −10.079 1.00 1.00 N ATOM 5387 C5 G B 7 −12.153 20.611 −9.054 1.00 1.00 C ATOM 5388 O6 G B 7 −11.342 21.402 −7.046 1.00 1.00 O ATOM 5389 C6 G B 7 −12.325 20.932 −7.642 1.00 1.00 C ATOM 5390 N1 G B 7 −13.586 20.654 −7.142 1.00 1.00 N ATOM 5391 N2 G B 7 −15.788 20.065 −7.313 1.00 1.00 N ATOM 5392 C2 G B 7 −14.613 20.196 −7.887 1.00 1.00 C ATOM 5393 N3 G B 7 −14.428 19.864 −9.077 1.00 1.00 N ATOM 5394 C4 G B 7 −13.140 20.057 −9.740 1.00 1.00 C ATOM 5395 H5*1 G B 7 −11.488 18.243 −15.345 1.00 1.00 H ATOM 5396 H5*2 G B 7 −12.200 19.667 −16.154 1.00 1.00 H ATOM 5397 H4* G B 7 −13.884 18.515 −14.728 1.00 1.00 H ATOM 5398 H1* G B 7 −14.276 18.485 −11.444 1.00 1.00 H ATOM 5399 H2*1 G B 7 −15.524 19.683 −13.102 1.00 1.00 H ATOM 5400 H2*2 G B 7 −14.974 21.042 −12.106 1.00 1.00 H ATOM 5401 H3* G B 7 −12.801 21.258 −13.602 1.00 1.00 H ATOM 5402 H8 G B 7 −11.021 20.576 −12.017 1.00 1.00 H ATOM 5403 H1 G B 7 −13.731 20.886 −6.174 1.00 1.00 H ATOM 5404 H21 G B 7 −16.529 19.735 −7.918 1.00 1.00 H ATOM 5405 H22 G B 7 −15.973 20.310 −6.337 1.00 1.00 H ATOM 5406 P C B 8 −15.013 22.538 −15.034 1.00 1.00 P ATOM 5407 O1P C B 8 −16.043 22.433 −16.113 1.00 1.00 O ATOM 5408 O2P C B 8 −13.947 23.570 −15.359 1.00 1.00 O ATOM 5409 O5* C B 8 −15.783 22.905 −13.691 1.00 1.00 O ATOM 5410 C5* C B 8 −17.195 22.716 −13.384 1.00 1.00 C ATOM 5411 C4* C B 8 −17.523 23.090 −11.904 1.00 1.00 C ATOM 5412 O4* C B 8 −16.493 22.558 −11.084 1.00 1.00 O ATOM 5413 C1* C B 8 −16.378 23.332 −9.935 1.00 1.00 C ATOM 5414 C2* C B 8 −16.908 24.778 −10.308 1.00 1.00 C ATOM 5415 C3* C B 8 −17.317 24.596 −11.774 1.00 1.00 C ATOM 5416 O3* C B 8 −18.514 25.243 −12.158 1.00 1.00 O ATOM 5417 N1 C B 8 −14.975 23.496 −9.588 1.00 1.00 N ATOM 5418 C6 C B 8 −14.006 23.448 −10.525 1.00 1.00 C ATOM 5419 C5 C B 8 −12.708 23.571 −10.200 1.00 1.00 C ATOM 5420 N4 C B 8 −11.045 23.957 −8.560 1.00 1.00 N ATOM 5421 C4 C B 8 −12.314 23.881 −8.840 1.00 1.00 C ATOM 5422 N3 C B 8 −13.228 23.990 −7.980 1.00 1.00 N ATOM 5423 O2 C B 8 −15.439 23.995 −7.385 1.00 1.00 O ATOM 5424 C2 C B 8 −14.646 23.864 −8.319 1.00 1.00 C ATOM 5425 H5*1 C B 8 −17.328 21.646 −13.529 1.00 1.00 H ATOM 5426 H5*2 C B 8 −17.927 23.210 −14.046 1.00 1.00 H ATOM 5427 H4* C B 8 −18.572 22.879 −11.608 1.00 1.00 H ATOM 5428 H1* C B 8 −16.927 22.835 −9.149 1.00 1.00 H ATOM 5429 H2*1 C B 8 −17.732 24.903 −9.615 1.00 1.00 H ATOM 5430 H2*2 C B 8 −16.148 25.607 −10.341 1.00 1.00 H ATOM 5431 H3* C B 8 −16.564 24.948 −12.437 1.00 1.00 H ATOM 5432 H6 C B 8 −14.227 23.270 −11.602 1.00 1.00 H ATOM 5433 H5 C B 8 −11.974 23.522 −11.001 1.00 1.00 H ATOM 5434 H41 C B 8 −10.754 24.151 −7.564 1.00 1.00 H ATOM 5435 H42 C B 8 −10.281 23.841 −9.293 1.00 1.00 H ATOM 5436 P G B 9 −18.789 26.828 −12.316 1.00 1.00 P ATOM 5437 O1P G B 9 −20.178 27.026 −12.741 1.00 1.00 O ATOM 5438 O2P G B 9 −17.741 27.664 −12.965 1.00 1.00 O ATOM 5439 O5* G B 9 −18.832 27.287 −10.786 1.00 1.00 O ATOM 5440 C5* G B 9 −19.889 27.068 −9.894 1.00 1.00 C ATOM 5441 C4* G B 9 −19.641 27.900 −8.611 1.00 1.00 C ATOM 5442 O4* G B 9 −18.346 27.598 −8.073 1.00 1.00 O ATOM 5443 C1* G B 9 −17.591 28.747 −7.830 1.00 1.00 C ATOM 5444 C2* G B 9 −18.220 29.831 −8.743 1.00 1.00 C ATOM 5445 C3* G B 9 −19.695 29.399 −8.929 1.00 1.00 C ATOM 5446 O3* G B 9 −20.601 30.061 −8.001 1.00 1.00 O ATOM 5447 N9 G B 9 −16.203 28.325 −8.032 1.00 1.00 N ATOM 5448 C8 G B 9 −15.746 28.016 −9.201 1.00 1.00 C ATOM 5449 N7 G B 9 −14.519 27.739 −9.094 1.00 1.00 N ATOM 5450 C5 G B 9 −14.086 27.936 −7.742 1.00 1.00 C ATOM 5451 O6 G B 9 −11.796 27.602 −7.445 1.00 1.00 O ATOM 5452 C6 G B 9 −12.856 27.908 −6.922 1.00 1.00 C ATOM 5453 N1 G B 9 −12.987 28.216 −5.621 1.00 1.00 N ATOM 5454 N2 G B 9 −14.134 28.801 −3.738 1.00 1.00 N ATOM 5455 C2 G B 9 −14.102 28.544 −5.021 1.00 1.00 C ATOM 5456 N3 G B 9 −15.189 28.579 −5.707 1.00 1.00 N ATOM 5457 C4 G B 9 −15.200 28.314 −7.138 1.00 1.00 C ATOM 5458 H5*1 G B 9 −19.897 26.001 −9.773 1.00 1.00 H ATOM 5459 H5*2 G B 9 −20.904 27.286 −10.243 1.00 1.00 H ATOM 5460 H4* G B 9 −20.493 27.668 −7.986 1.00 1.00 H ATOM 5461 H1* G B 9 −17.779 29.094 −6.784 1.00 1.00 H ATOM 5462 H2*1 G B 9 −18.114 30.826 −8.268 1.00 1.00 H ATOM 5463 H2*2 G B 9 −17.673 29.813 −9.697 1.00 1.00 H ATOM 5464 H3* G B 9 −20.015 29.601 −9.962 1.00 1.00 H ATOM 5465 H8 G B 9 −16.314 27.961 −10.108 1.00 1.00 H ATOM 5466 H1 G B 9 −12.110 28.116 −5.121 1.00 1.00 H ATOM 5467 H21 G B 9 −15.028 29.144 −3.313 1.00 1.00 H ATOM 5468 H22 G B 9 −13.284 28.700 −3.156 1.00 1.00 H ATOM 5469 P C B 10 −20.868 31.636 −8.095 1.00 1.00 P ATOM 5470 O1P C B 10 −22.094 31.996 −7.319 1.00 1.00 O ATOM 5471 O2P C B 10 −21.176 32.136 −9.466 1.00 1.00 O ATOM 5472 O5* C B 10 −19.589 32.264 −7.457 1.00 1.00 O ATOM 5473 C5* C B 10 −19.587 32.170 −6.031 1.00 1.00 C ATOM 5474 C4* C B 10 −18.234 32.618 −5.427 1.00 1.00 C ATOM 5475 O4* C B 10 −17.161 31.747 −5.882 1.00 1.00 O ATOM 5476 C1* C B 10 −15.928 32.412 −5.519 1.00 1.00 C ATOM 5477 C2* C B 10 −16.244 33.921 −5.479 1.00 1.00 C ATOM 5478 C3* C B 10 −17.758 34.026 −5.851 1.00 1.00 C ATOM 5479 O3* C B 10 −18.438 34.942 −5.015 1.00 1.00 O ATOM 5480 N1 C B 10 −14.974 32.009 −6.543 1.00 1.00 N ATOM 5481 C6 C B 10 −15.334 31.783 −7.832 1.00 1.00 C ATOM 5482 C5 C B 10 −14.504 31.274 −8.746 1.00 1.00 C ATOM 5483 N4 C B 10 −12.215 30.493 −9.197 1.00 1.00 N ATOM 5484 C4 C B 10 −13.099 30.948 −8.353 1.00 1.00 C ATOM 5485 N3 C B 10 −12.782 31.195 −7.157 1.00 1.00 N ATOM 5486 O2 C B 10 −13.330 31.894 −5.025 1.00 1.00 O ATOM 5487 C2 C B 10 −13.693 31.747 −6.183 1.00 1.00 C ATOM 5488 H5*1 C B 10 −19.750 31.127 −5.738 1.00 1.00 H ATOM 5489 H5*2 C B 10 −20.401 32.754 −5.639 1.00 1.00 H ATOM 5490 H4* C B 10 −18.231 32.619 −4.335 1.00 1.00 H ATOM 5491 H1* C B 10 −15.752 31.976 −4.493 1.00 1.00 H ATOM 5492 H2*1 C B 10 −16.119 34.314 −4.465 1.00 1.00 H ATOM 5493 H2*2 C B 10 −15.586 34.527 −6.168 1.00 1.00 H ATOM 5494 H3* C B 10 −17.962 34.301 −6.906 1.00 1.00 H ATOM 5495 H6 C B 10 −16.315 32.055 −8.126 1.00 1.00 H ATOM 5496 H5 C B 10 −14.816 31.091 −9.769 1.00 1.00 H ATOM 5497 H41 C B 10 −11.203 30.370 −8.919 1.00 1.00 H ATOM 5498 H42 C B 10 −12.493 30.353 −10.167 1.00 1.00 H ATOM 5499 P T B 11 −18.279 36.516 −5.075 1.00 1.00 P ATOM 5500 O1P T B 11 −19.363 37.115 −4.226 1.00 1.00 O ATOM 5501 O2P T B 11 −18.482 36.915 −6.493 1.00 1.00 O ATOM 5502 O5* T B 11 −16.793 36.910 −4.660 1.00 1.00 O ATOM 5503 C5* T B 11 −16.357 37.084 −3.309 1.00 1.00 C ATOM 5504 C4* T B 11 −14.832 37.055 −3.440 1.00 1.00 C ATOM 5505 O4* T B 11 −14.273 35.984 −4.219 1.00 1.00 O ATOM 5506 C1* T B 11 −12.956 36.338 −4.625 1.00 1.00 C ATOM 5507 C2* T B 11 −12.976 37.890 −4.772 1.00 1.00 C ATOM 5508 C3* T B 11 −14.291 38.381 −4.071 1.00 1.00 C ATOM 5509 O3* T B 11 −14.074 39.278 −2.958 1.00 1.00 O ATOM 5510 N1 T B 11 −12.650 35.651 −5.866 1.00 1.00 N ATOM 5511 C6 T B 11 −13.576 35.693 −6.870 1.00 1.00 C ATOM 5512 C5M T B 11 −14.499 35.102 −9.088 1.00 1.00 C ATOM 5513 C5 T B 11 −13.418 35.051 −8.047 1.00 1.00 C ATOM 5514 O4 T B 11 −11.879 33.791 −9.285 1.00 1.00 O ATOM 5515 C4 T B 11 −12.126 34.332 −8.222 1.00 1.00 C ATOM 5516 N3 T B 11 −11.277 34.282 −7.192 1.00 1.00 N ATOM 5517 O2 T B 11 −10.662 34.801 −5.083 1.00 1.00 O ATOM 5518 C2 T B 11 −11.476 34.922 −5.995 1.00 1.00 C ATOM 5519 H5*1 T B 11 −16.698 36.180 −2.794 1.00 1.00 H ATOM 5520 H5*2 T B 11 −16.792 37.930 −2.754 1.00 1.00 H ATOM 5521 H4* T B 11 −14.429 36.883 −2.427 1.00 1.00 H ATOM 5522 H1* T B 11 −12.277 36.042 −3.793 1.00 1.00 H ATOM 5523 H2*1 T B 11 −12.156 38.288 −4.177 1.00 1.00 H ATOM 5524 H2*2 T B 11 −12.967 38.234 −5.798 1.00 1.00 H ATOM 5525 H3* T B 11 −15.092 38.843 −4.705 1.00 1.00 H ATOM 5526 H6 T B 11 −14.525 36.230 −6.847 1.00 1.00 H ATOM 5527 H51 T B 11 −14.117 35.443 −10.085 1.00 1.00 H ATOM 5528 H52 T B 11 −14.785 34.065 −9.271 1.00 1.00 H ATOM 5529 H53 T B 11 −15.415 35.686 −8.986 1.00 1.00 H ATOM 5530 H3 T B 11 −10.496 33.752 −7.471 1.00 1.00 H ATOM 5531 P C B 12 −13.415 40.706 −2.886 1.00 1.00 P ATOM 5532 O1P C B 12 −13.642 41.103 −1.467 1.00 1.00 O ATOM 5533 O2P C B 12 −14.098 41.613 −3.866 1.00 1.00 O ATOM 5534 O5* C B 12 −11.843 40.616 −3.145 1.00 1.00 O ATOM 5535 C5* C B 12 −10.814 40.226 −2.254 1.00 1.00 C ATOM 5536 C4* C B 12 −9.533 40.006 −3.032 1.00 1.00 C ATOM 5537 O4* C B 12 −9.828 39.108 −4.120 1.00 1.00 O ATOM 5538 C1* C B 12 −8.793 39.119 −5.112 1.00 1.00 C ATOM 5539 C2* C B 12 −8.527 40.652 −5.180 1.00 1.00 C ATOM 5540 C3* C B 12 −9.043 41.210 −3.828 1.00 1.00 C ATOM 5541 O3* C B 12 −8.024 41.758 −3.056 1.00 1.00 O ATOM 5542 N1 C B 12 −9.340 38.646 −6.376 1.00 1.00 N ATOM 5543 C6 C B 12 −10.544 39.083 −6.828 1.00 1.00 C ATOM 5544 C5 C B 12 −11.132 38.633 −7.960 1.00 1.00 C ATOM 5545 N4 C B 12 −10.987 37.086 −9.833 1.00 1.00 N ATOM 5546 C4 C B 12 −10.507 37.585 −8.729 1.00 1.00 C ATOM 5547 N3 C B 12 −9.350 37.240 −8.359 1.00 1.00 N ATOM 5548 O2 C B 12 −7.532 37.374 −7.017 1.00 1.00 O ATOM 5549 C2 C B 12 −8.700 37.720 −7.139 1.00 1.00 C ATOM 5550 H5*1 C B 12 −11.151 39.385 −1.598 1.00 1.00 H ATOM 5551 H5*2 C B 12 −10.687 41.048 −1.556 1.00 1.00 H ATOM 5552 H4* C B 12 −8.752 39.564 −2.367 1.00 1.00 H ATOM 5553 H1* C B 12 −7.939 38.522 −4.753 1.00 1.00 H ATOM 5554 H2*1 C B 12 −7.496 40.835 −5.312 1.00 1.00 H ATOM 5555 H2*2 C B 12 −9.129 41.158 −5.971 1.00 1.00 H ATOM 5556 H3* C B 12 −9.932 41.872 −4.071 1.00 1.00 H ATOM 5557 H6 C B 12 −11.048 39.851 −6.222 1.00 1.00 H ATOM 5558 H5 C B 12 −12.083 39.029 −8.265 1.00 1.00 H ATOM 5559 H41 C B 12 −10.412 36.479 −10.450 1.00 1.00 H ATOM 5560 H42 C B 12 −11.906 37.388 −10.178 1.00 1.00 H ATOM 5561 P G B 13 −7.073 43.034 −3.229 1.00 1.00 P ATOM 5562 O1P G B 13 −6.297 43.476 −2.031 1.00 1.00 O ATOM 5563 O2P G B 13 −7.802 44.182 −3.858 1.00 1.00 O ATOM 5564 O5* G B 13 −5.904 42.576 −4.284 1.00 1.00 O ATOM 5565 C5* G B 13 −4.859 41.753 −3.818 1.00 1.00 C ATOM 5566 C4* G B 13 −3.974 41.438 −5.065 1.00 1.00 C ATOM 5567 O4* G B 13 −4.793 40.766 −6.057 1.00 1.00 O ATOM 5568 C1* G B 13 −4.535 41.391 −7.341 1.00 1.00 C ATOM 5569 C2* G B 13 −4.284 42.898 −6.955 1.00 1.00 C ATOM 5570 C3* G B 13 −3.412 42.750 −5.683 1.00 1.00 C ATOM 5571 O3* G B 13 −2.080 42.382 −6.130 1.00 1.00 O ATOM 5572 N9 G B 13 −5.677 41.168 −8.227 1.00 1.00 N ATOM 5573 C8 G B 13 −6.843 41.756 −8.064 1.00 1.00 C ATOM 5574 N7 G B 13 −7.637 41.377 −8.968 1.00 1.00 N ATOM 5575 C5 G B 13 −6.989 40.374 −9.757 1.00 1.00 C ATOM 5576 O6 G B 13 −8.544 39.475 −11.238 1.00 1.00 O ATOM 5577 C6 G B 13 −7.384 39.551 −10.884 1.00 1.00 C ATOM 5578 N1 G B 13 −6.342 38.812 −11.396 1.00 1.00 N ATOM 5579 N2 G B 13 −4.181 38.090 −11.521 1.00 1.00 N ATOM 5580 C2 G B 13 −5.060 38.825 −10.921 1.00 1.00 C ATOM 5581 N3 G B 13 −4.746 39.470 −9.877 1.00 1.00 N ATOM 5582 C4 G B 13 −5.770 40.320 −9.243 1.00 1.00 C ATOM 5583 H5*1 G B 13 −5.397 40.818 −3.475 1.00 1.00 H ATOM 5584 H5*2 G B 13 −4.170 42.094 −3.068 1.00 1.00 H ATOM 5585 H4* G B 13 −3.115 40.786 −4.876 1.00 1.00 H ATOM 5586 H1* G B 13 −3.729 40.852 −7.891 1.00 1.00 H ATOM 5587 H2*1 G B 13 −3.788 43.453 −7.719 1.00 1.00 H ATOM 5588 H2*2 G B 13 −5.234 43.527 −6.763 1.00 1.00 H ATOM 5589 H3* G B 13 −3.402 43.611 −5.019 1.00 1.00 H ATOM 5590 H8 G B 13 −7.186 42.491 −7.351 1.00 1.00 H ATOM 5591 H1 G B 13 −6.591 38.261 −12.223 1.00 1.00 H ATOM 5592 H21 G B 13 −3.216 37.998 −11.125 1.00 1.00 H ATOM 5593 H22 G B 13 −4.417 37.621 −12.389 1.00 1.00 H ATOM 5594 P A B 14 −0.974 43.331 −6.757 1.00 1.00 P ATOM 5595 O1P A B 14 0.147 43.235 −5.788 1.00 1.00 O ATOM 5596 O2P A B 14 −1.472 44.751 −6.655 1.00 1.00 O ATOM 5597 O5* A B 14 −0.623 42.891 −8.251 1.00 1.00 O ATOM 5598 C5* A B 14 0.267 41.766 −8.359 1.00 1.00 C ATOM 5599 C4* A B 14 0.314 41.376 −9.873 1.00 1.00 C ATOM 5600 O4* A B 14 −1.048 40.979 −10.210 1.00 1.00 O ATOM 5601 C1* A B 14 −1.349 41.351 −11.568 1.00 1.00 C ATOM 5602 C2* A B 14 −0.416 42.533 −11.868 1.00 1.00 C ATOM 5603 C3* A B 14 0.722 42.546 −10.835 1.00 1.00 C ATOM 5604 O3* A B 14 1.981 42.171 −11.453 1.00 1.00 O ATOM 5605 N9 A B 14 −2.777 41.736 −11.686 1.00 1.00 N ATOM 5606 C8 A B 14 −3.393 42.442 −10.799 1.00 1.00 C ATOM 5607 N7 A B 14 −4.627 42.559 −11.041 1.00 1.00 N ATOM 5608 C5 A B 14 −4.926 41.880 −12.201 1.00 1.00 C ATOM 5609 N6 A B 14 −7.298 42.162 −12.605 1.00 1.00 N ATOM 5610 C6 A B 14 −6.059 41.644 −12.950 1.00 1.00 C ATOM 5611 N1 A B 14 −5.893 40.830 −14.024 1.00 1.00 N ATOM 5612 C2 A B 14 −4.714 40.179 −14.298 1.00 1.00 C ATOM 5613 N3 A B 14 −3.618 40.506 −13.598 1.00 1.00 N ATOM 5614 C4 A B 14 −3.697 41.358 −12.585 1.00 1.00 C ATOM 5615 H5*1 A B 14 −0.070 40.993 −7.669 1.00 1.00 H ATOM 5616 H5*2 A B 14 1.258 42.090 −8.054 1.00 1.00 H ATOM 5617 H4* A B 14 1.017 40.523 −10.041 1.00 1.00 H ATOM 5618 H1* A B 14 −1.126 40.492 −12.184 1.00 1.00 H ATOM 5619 H2*1 A B 14 0.042 42.568 −12.867 1.00 1.00 H ATOM 5620 H2*2 A B 14 −0.979 43.504 −11.787 1.00 1.00 H ATOM 5621 H3* A B 14 0.770 43.486 −10.207 1.00 1.00 H ATOM 5622 H8 A B 14 −2.827 42.787 −9.970 1.00 1.00 H ATOM 5623 H61 A B 14 −7.406 42.643 −11.681 1.00 1.00 H ATOM 5624 H62 A B 14 −8.115 41.987 −13.191 1.00 1.00 H ATOM 5625 H2 A B 14 −4.637 39.457 −15.074 1.00 1.00 H ATOM 5626 P A B 15 2.802 42.972 −12.572 1.00 1.00 P ATOM 5627 O1P A B 15 4.188 42.421 −12.603 1.00 1.00 O ATOM 5628 O2P A B 15 2.881 44.321 −12.020 1.00 1.00 O ATOM 5629 O5* A B 15 2.170 42.882 −14.040 1.00 1.00 O ATOM 5630 C5* A B 15 2.031 41.643 −14.749 1.00 1.00 C ATOM 5631 C4* A B 15 1.120 41.842 −15.968 1.00 1.00 C ATOM 5632 O4* A B 15 −0.159 42.194 −15.418 1.00 1.00 O ATOM 5633 C1* A B 15 −0.768 43.197 −16.209 1.00 1.00 C ATOM 5634 C2* A B 15 0.453 44.129 −16.425 1.00 1.00 C ATOM 5635 C3* A B 15 1.490 43.056 −16.860 1.00 1.00 C ATOM 5636 O3* A B 15 1.154 42.647 −18.183 1.00 1.00 O ATOM 5637 N9 A B 15 −1.824 43.770 −15.348 1.00 1.00 N ATOM 5638 C8 A B 15 −1.738 44.435 −14.218 1.00 1.00 C ATOM 5639 N7 A B 15 −2.903 44.749 −13.791 1.00 1.00 N ATOM 5640 C5 A B 15 −3.865 44.242 −14.573 1.00 1.00 C ATOM 5641 N6 A B 15 −5.818 44.901 −13.515 1.00 1.00 N ATOM 5642 C6 A B 15 −5.252 44.343 −14.589 1.00 1.00 C ATOM 5643 N1 A B 15 −5.855 43.927 −15.707 1.00 1.00 N ATOM 5644 C2 A B 15 −5.205 43.155 −16.606 1.00 1.00 C ATOM 5645 N3 A B 15 −3.874 42.988 −16.576 1.00 1.00 N ATOM 5646 C4 A B 15 −3.171 43.579 −15.600 1.00 1.00 C ATOM 5647 H5*1 A B 15 1.565 40.899 −14.050 1.00 1.00 H ATOM 5648 H5*2 A B 15 3.024 41.294 −15.047 1.00 1.00 H ATOM 5649 H4* A B 15 1.095 40.898 −16.542 1.00 1.00 H ATOM 5650 H1* A B 15 −1.184 42.882 −17.172 1.00 1.00 H ATOM 5651 H2*1 A B 15 0.327 44.839 −17.249 1.00 1.00 H ATOM 5652 H2*2 A B 15 0.758 44.690 −15.550 1.00 1.00 H ATOM 5653 H3* A B 15 2.535 43.337 −16.677 1.00 1.00 H ATOM 5654 H8 A B 15 −0.821 44.738 −13.674 1.00 1.00 H ATOM 5655 H61 A B 15 −5.235 45.212 −12.697 1.00 1.00 H ATOM 5656 H62 A B 15 −6.839 44.805 −13.371 1.00 1.00 H ATOM 5657 H2 A B 15 −5.818 42.644 −17.364 1.00 1.00 H ATOM 5658 H9 A B 15 1.328 43.353 −18.798 1.00 1.00 H TER HETATM 5659 H5*1 DRG C 1 −6.234 4.404 −4.753 1.00 1.00 H HETATM 5660 H5*2 DRG C 1 −7.640 5.215 −5.457 1.00 1.00 H HETATM 5661 H4* DRG C 1 −5.518 6.203 −6.211 1.00 1.00 H HETATM 5662 H1* DRG C 1 −4.682 9.088 −5.766 1.00 1.00 H HETATM 5663 H2*1 DRG C 1 −3.036 7.500 −5.113 1.00 1.00 H HETATM 5664 H2*2 DRG C 1 −3.432 7.765 −3.331 1.00 1.00 H HETATM 5665 H3* DRG C 1 −4.886 5.962 −3.282 1.00 1.00 H HETATM 5666 H8 DRG C 1 −7.116 8.923 −3.087 1.00 1.00 H HETATM 5667 H61 DRG C 1 −6.048 12.553 −0.414 1.00 1.00 H HETATM 5668 H62 DRG C 1 −4.643 13.636 −0.176 1.00 1.00 H HETATM 5669 H2 DRG C 1 −1.642 12.255 −3.458 1.00 1.00 H HETATM 5670 O1 DRG C 1 −6.465 4.206 −1.473 1.00 1.00 O HETATM 5671 H3 DRG C 1 −3.408 5.274 −5.618 1.00 1.00 H HETATM 5672 P DRG C 1 −7.712 4.826 −2.256 1.00 1.00 P HETATM 5673 O1P DRG C 1 −8.592 5.594 −1.295 1.00 1.00 O HETATM 5674 O2P DRG C 1 −8.561 3.811 −2.977 1.00 1.00 O HETATM 5675 O5* DRG C 1 −7.262 5.761 −3.432 1.00 1.00 O HETATM 5676 C5* DRG C 1 −6.840 5.335 −4.712 1.00 1.00 C HETATM 5677 C4* DRG C 1 −5.821 6.420 −5.169 1.00 1.00 C HETATM 5678 O4* DRG C 1 −6.218 7.779 −4.952 1.00 1.00 O HETATM 5679 C1* DRG C 1 −4.947 8.538 −4.797 1.00 1.00 C HETATM 5680 C2* DRG C 1 −3.853 7.586 −4.341 1.00 1.00 C HETATM 5681 C3* DRG C 1 −4.533 6.224 −4.325 1.00 1.00 C HETATM 5682 O3* DRG C 1 −3.692 5.130 −4.720 1.00 1.00 O HETATM 5683 N9 DRG C 1 −5.231 9.507 −3.766 1.00 1.00 N HETATM 5684 C8 DRG C 1 −6.272 9.528 −3.047 1.00 1.00 C HETATM 5685 N7 DRG C 1 −6.158 10.412 −2.154 1.00 1.00 N HETATM 5686 C5 DRG C 1 −5.018 11.103 −2.345 1.00 1.00 C HETATM 5687 N6 DRG C 1 −5.085 12.834 −0.637 1.00 1.00 N HETATM 5688 C6 DRG C 1 −4.479 12.217 −1.694 1.00 1.00 C HETATM 5689 N1 DRG C 1 −3.292 12.621 −2.168 1.00 1.00 N HETATM 5690 C2 DRG C 1 −2.646 11.967 −3.180 1.00 1.00 C HETATM 5691 N3 DRG C 1 −3.200 10.926 −3.832 1.00 1.00 N HETATM 5692 C4 DRG C 1 −4.378 10.496 −3.400 1.00 1.00 C HETATM 5693 P12 DRG C 1 −5.757 2.877 −2.006 1.00 1.00 P HETATM 5694 O12 DRG C 1 −6.628 2.525 −3.129 1.00 1.00 O HETATM 5695 O13 DRG C 1 −4.368 2.965 −2.594 1.00 1.00 O HETATM 5696 O14 DRG C 1 −5.954 1.686 −0.980 1.00 1.00 O HETATM 5697 P12 DRG C 1 −7.421 1.164 −0.904 1.00 1.00 P HETATM 5698 O12 DRG C 1 −7.795 0.208 0.168 1.00 1.00 O HETATM 5699 O13 DRG C 1 −8.524 2.044 −1.374 1.00 1.00 O HETATM 5700 O14 DRG C 1 −7.878 0.803 −2.282 1.00 1.00 O TER ATOM 5701 P T D 1 −16.243 44.859 −18.466 1.00 1.00 P ATOM 5702 O1P T D 1 −15.981 46.317 −18.398 1.00 1.00 O ATOM 5703 O2P T D 1 −17.352 44.483 −19.420 1.00 1.00 O ATOM 5704 O5* T D 1 −14.832 44.218 −18.868 1.00 1.00 O ATOM 5705 C5* T D 1 −14.342 44.382 −20.210 1.00 1.00 C ATOM 5706 C4* T D 1 −12.864 43.864 −20.288 1.00 1.00 C ATOM 5707 O4* T D 1 −12.002 44.648 −19.443 1.00 1.00 O ATOM 5708 C1* T D 1 −10.766 43.887 −19.189 1.00 1.00 C ATOM 5709 C2* T D 1 −11.059 42.405 −19.588 1.00 1.00 C ATOM 5710 C3* T D 1 −12.609 42.444 −19.799 1.00 1.00 C ATOM 5711 O3* T D 1 −13.085 41.480 −20.721 1.00 1.00 O ATOM 5712 N1 T D 1 −10.333 44.120 −17.843 1.00 1.00 N ATOM 5713 C6 T D 1 −11.192 44.693 −16.964 1.00 1.00 C ATOM 5714 C5M T D 1 −11.609 45.628 −14.657 1.00 1.00 C ATOM 5715 C5 T D 1 −10.813 44.955 −15.700 1.00 1.00 C ATOM 5716 O4 T D 1 −9.026 44.806 −14.152 1.00 1.00 O ATOM 5717 C4 T D 1 −9.440 44.585 −15.281 1.00 1.00 C ATOM 5718 N3 T D 1 −8.643 43.979 −16.206 1.00 1.00 N ATOM 5719 O2 T D 1 −8.246 43.474 −18.290 1.00 1.00 O ATOM 5720 C2 T D 1 −9.069 43.818 −17.478 1.00 1.00 C ATOM 5721 H5*1 T D 1 −14.331 45.478 −20.389 1.00 1.00 H ATOM 5722 H5*2 T D 1 −15.053 43.979 −20.941 1.00 1.00 H ATOM 5723 H4* T D 1 −12.472 43.952 −21.370 1.00 1.00 H ATOM 5724 H1* T D 1 −9.908 44.287 −19.814 1.00 1.00 H ATOM 5725 H2*1 T D 1 −10.558 42.206 −20.542 1.00 1.00 H ATOM 5726 H2*2 T D 1 −10.661 41.605 −18.974 1.00 1.00 H ATOM 5727 H3* T D 1 −13.066 42.351 −18.795 1.00 1.00 H ATOM 5728 H6 T D 1 −12.210 45.079 −17.201 1.00 1.00 H ATOM 5729 H51 T D 1 −11.410 46.728 −14.678 1.00 1.00 H ATOM 5730 H52 T D 1 −12.668 45.494 −14.745 1.00 1.00 H ATOM 5731 H53 T D 1 −11.352 45.216 −13.697 1.00 1.00 H ATOM 5732 H3 T D 1 −7.705 43.640 −15.928 1.00 1.00 H ATOM 5733 H10 T D 1 −16.450 44.625 −17.502 1.00 1.00 H ATOM 5734 P T D 2 −13.141 39.897 −20.668 1.00 1.00 P ATOM 5735 O1P T D 2 −13.867 39.327 −21.867 1.00 1.00 O ATOM 5736 O2P T D 2 −13.779 39.372 −19.436 1.00 1.00 O ATOM 5737 O5* T D 2 −11.632 39.399 −20.790 1.00 1.00 O ATOM 5738 C5* T D 2 −10.592 39.382 −21.789 1.00 1.00 C ATOM 5739 C4* T D 2 −9.268 38.934 −21.167 1.00 1.00 C ATOM 5740 O4* T D 2 −8.991 39.812 −20.107 1.00 1.00 O ATOM 5741 C1* T D 2 −8.246 39.047 −19.100 1.00 1.00 C ATOM 5742 C2* T D 2 −8.761 37.545 −19.130 1.00 1.00 C ATOM 5743 C3* T D 2 −9.363 37.500 −20.590 1.00 1.00 C ATOM 5744 O3* T D 2 −8.718 36.581 −21.484 1.00 1.00 O ATOM 5745 N1 T D 2 −8.584 39.583 −17.816 1.00 1.00 N ATOM 5746 C6 T D 2 −9.946 39.723 −17.505 1.00 1.00 C ATOM 5747 C5M T D 2 −11.751 40.621 −16.089 1.00 1.00 C ATOM 5748 C5 T D 2 −10.294 40.349 −16.375 1.00 1.00 C ATOM 5749 O4 T D 2 −9.635 41.444 −14.420 1.00 1.00 O ATOM 5750 C4 T D 2 −9.277 40.831 −15.423 1.00 1.00 C ATOM 5751 N3 T D 2 −7.989 40.616 −15.779 1.00 1.00 N ATOM 5752 O2 T D 2 −6.475 40.024 −17.274 1.00 1.00 O ATOM 5753 C2 T D 2 −7.666 40.078 −16.969 1.00 1.00 C ATOM 5754 H5*1 T D 2 −10.389 40.377 −22.227 1.00 1.00 H ATOM 5755 H5*2 T D 2 −10.896 38.692 −22.671 1.00 1.00 H ATOM 5756 H4* T D 2 −8.408 38.930 −21.886 1.00 1.00 H ATOM 5757 H1* T D 2 −7.209 39.123 −19.408 1.00 1.00 H ATOM 5758 H2*1 T D 2 −7.827 36.907 −18.990 1.00 1.00 H ATOM 5759 H2*2 T D 2 −9.482 37.317 −18.346 1.00 1.00 H ATOM 5760 H3* T D 2 −10.401 37.123 −20.490 1.00 1.00 H ATOM 5761 H6 T D 2 −10.702 39.367 −18.213 1.00 1.00 H ATOM 5762 H51 T D 2 −11.907 41.728 −15.904 1.00 1.00 H ATOM 5763 H52 T D 2 −12.322 40.362 −17.012 1.00 1.00 H ATOM 5764 H53 T D 2 −12.139 39.972 −15.256 1.00 1.00 H ATOM 5765 H3 T D 2 −7.281 40.874 −15.170 1.00 1.00 H ATOM 5766 P C D 3 −8.448 34.971 −21.337 1.00 1.00 P ATOM 5767 O1P C D 3 −7.679 34.400 −22.490 1.00 1.00 O ATOM 5768 O2P C D 3 −9.781 34.262 −21.219 1.00 1.00 O ATOM 5769 O5* C D 3 −7.434 34.614 −20.122 1.00 1.00 O ATOM 5770 C5* C D 3 −6.022 34.909 −20.312 1.00 1.00 C ATOM 5771 C4* C D 3 −5.324 34.967 −18.928 1.00 1.00 C ATOM 5772 O4* C D 3 −5.903 36.023 −18.087 1.00 1.00 O ATOM 5773 C1* C D 3 −5.548 35.700 −16.772 1.00 1.00 C ATOM 5774 C2* C D 3 −5.670 34.147 −16.741 1.00 1.00 C ATOM 5775 C3* C D 3 −5.530 33.660 −18.198 1.00 1.00 C ATOM 5776 O3* C D 3 −4.393 32.862 −18.477 1.00 1.00 O ATOM 5777 N1 C D 3 −6.597 36.322 −15.965 1.00 1.00 N ATOM 5778 C6 C D 3 −7.938 36.212 −16.241 1.00 1.00 C ATOM 5779 C5 C D 3 −8.866 36.871 −15.557 1.00 1.00 C ATOM 5780 N4 C D 3 −9.363 38.397 −13.748 1.00 1.00 N ATOM 5781 C4 C D 3 −8.446 37.675 −14.377 1.00 1.00 C ATOM 5782 N3 C D 3 −7.240 37.665 −14.024 1.00 1.00 N ATOM 5783 O2 C D 3 −5.122 37.022 −14.336 1.00 1.00 O ATOM 5784 C2 C D 3 −6.260 36.949 −14.794 1.00 1.00 C ATOM 5785 H5*1 C D 3 −6.065 35.893 −20.778 1.00 1.00 H ATOM 5786 H5*2 C D 3 −5.502 34.266 −20.980 1.00 1.00 H ATOM 5787 H4* C D 3 −4.197 35.194 −19.014 1.00 1.00 H ATOM 5788 H1* C D 3 −4.501 36.070 −16.502 1.00 1.00 H ATOM 5789 H2*1 C D 3 −4.832 33.835 −16.143 1.00 1.00 H ATOM 5790 H2*2 C D 3 −6.586 33.834 −16.247 1.00 1.00 H ATOM 5791 H3* C D 3 −6.506 33.214 −18.523 1.00 1.00 H ATOM 5792 H6 C D 3 −8.239 35.621 −17.104 1.00 1.00 H ATOM 5793 H5 C D 3 −9.877 36.860 −15.869 1.00 1.00 H ATOM 5794 H41 C D 3 −9.106 38.950 −12.937 1.00 1.00 H ATOM 5795 H42 C D 3 −10.331 38.394 −14.074 1.00 1.00 H ATOM 5796 P G D 4 −3.845 31.501 −17.802 1.00 1.00 P ATOM 5797 O1P G D 4 −2.595 31.040 −18.476 1.00 1.00 O ATOM 5798 O2P G D 4 −4.922 30.498 −17.944 1.00 1.00 O ATOM 5799 O5* G D 4 −3.351 31.774 −16.299 1.00 1.00 O ATOM 5800 C5* G D 4 −2.175 32.555 −15.920 1.00 1.00 C ATOM 5801 C4* G D 4 −2.219 32.938 −14.460 1.00 1.00 C ATOM 5802 O4* G D 4 −3.463 33.619 −14.269 1.00 1.00 O ATOM 5803 C1* G D 4 −3.811 33.531 −12.854 1.00 1.00 C ATOM 5804 C2* G D 4 −3.504 32.096 −12.443 1.00 1.00 C ATOM 5805 C3* G D 4 −2.327 31.764 −13.437 1.00 1.00 C ATOM 5806 O3* G D 4 −1.042 31.561 −12.831 1.00 1.00 O ATOM 5807 N9 G D 4 −5.248 33.785 −12.718 1.00 1.00 N ATOM 5808 C8 G D 4 −6.150 33.270 −13.510 1.00 1.00 C ATOM 5809 N7 G D 4 −7.277 33.714 −13.212 1.00 1.00 N ATOM 5810 C5 G D 4 −7.131 34.630 −12.128 1.00 1.00 C ATOM 5811 O6 G D 4 −9.213 35.446 −11.535 1.00 1.00 O ATOM 5812 C6 G D 4 −8.000 35.489 −11.338 1.00 1.00 C ATOM 5813 N1 G D 4 −7.412 36.205 −10.388 1.00 1.00 N ATOM 5814 N2 G D 4 −5.600 36.721 −9.057 1.00 1.00 N ATOM 5815 C2 G D 4 −6.071 36.066 −10.094 1.00 1.00 C ATOM 5816 N3 G D 4 −5.317 35.274 −10.745 1.00 1.00 N ATOM 5817 C4 G D 4 −5.867 34.541 −11.849 1.00 1.00 C ATOM 5818 H5*1 G D 4 −2.067 33.508 −16.507 1.00 1.00 H ATOM 5819 H5*2 G D 4 −1.276 32.004 −16.217 1.00 1.00 H ATOM 5820 H4* G D 4 −1.371 33.585 −14.200 1.00 1.00 H ATOM 5821 H1* G D 4 −3.265 34.301 −12.232 1.00 1.00 H ATOM 5822 H2*1 G D 4 −3.168 32.086 −11.421 1.00 1.00 H ATOM 5823 H2*2 G D 4 −4.436 31.527 −12.517 1.00 1.00 H ATOM 5824 H3* G D 4 −2.603 30.854 −13.926 1.00 1.00 H ATOM 5825 H8 G D 4 −6.022 32.557 −14.353 1.00 1.00 H ATOM 5826 H1 G D 4 −7.970 36.736 −9.870 1.00 1.00 H ATOM 5827 H21 G D 4 −4.590 36.663 −8.848 1.00 1.00 H ATOM 5828 H22 G D 4 −6.225 37.206 −8.390 1.00 1.00 H ATOM 5829 P A D 5 −0.638 30.399 −11.761 1.00 1.00 P ATOM 5830 O1P A D 5 0.865 30.376 −11.845 1.00 1.00 O ATOM 5831 O2P A D 5 −1.276 29.073 −11.979 1.00 1.00 O ATOM 5832 O5* A D 5 −1.042 30.957 −10.328 1.00 1.00 O ATOM 5833 C5* A D 5 −0.461 32.189 −9.805 1.00 1.00 C ATOM 5834 C4* A D 5 −1.310 32.726 −8.600 1.00 1.00 C ATOM 5835 O4* A D 5 −2.631 32.989 −9.008 1.00 1.00 O ATOM 5836 C1* A D 5 −3.588 32.785 −7.964 1.00 1.00 C ATOM 5837 C2* A D 5 −3.011 31.503 −7.317 1.00 1.00 C ATOM 5838 C3* A D 5 −1.510 31.644 −7.517 1.00 1.00 C ATOM 5839 O3* A D 5 −0.711 32.149 −6.364 1.00 1.00 O ATOM 5840 N9 A D 5 −4.928 32.556 −8.467 1.00 1.00 N ATOM 5841 C8 A D 5 −5.210 31.756 −9.442 1.00 1.00 C ATOM 5842 N7 A D 5 −6.436 31.804 −9.707 1.00 1.00 N ATOM 5843 C5 A D 5 −7.059 32.694 −8.933 1.00 1.00 C ATOM 5844 N6 A D 5 −9.220 32.767 −9.873 1.00 1.00 N ATOM 5845 C6 A D 5 −8.357 33.186 −8.912 1.00 1.00 C ATOM 5846 N1 A D 5 −8.675 33.979 −7.867 1.00 1.00 N ATOM 5847 C2 A D 5 −7.758 34.249 −6.907 1.00 1.00 C ATOM 5848 N3 A D 5 −6.454 33.898 −7.006 1.00 1.00 N ATOM 5849 C4 A D 5 −6.088 33.148 −8.055 1.00 1.00 C ATOM 5850 H5*1 A D 5 −0.467 32.942 −10.606 1.00 1.00 H ATOM 5851 H5*2 A D 5 0.594 32.054 −9.476 1.00 1.00 H ATOM 5852 H4* A D 5 −0.880 33.689 −8.233 1.00 1.00 H ATOM 5853 H1* A D 5 −3.565 33.636 −7.249 1.00 1.00 H ATOM 5854 H2*1 A D 5 −3.226 31.457 −6.272 1.00 1.00 H ATOM 5855 H2*2 A D 5 −3.402 30.591 −7.799 1.00 1.00 H ATOM 5856 H3* A D 5 −1.097 30.643 −7.734 1.00 1.00 H ATOM 5857 H8 A D 5 −4.465 31.101 −9.906 1.00 1.00 H ATOM 5858 H61 A D 5 −8.886 32.245 −10.707 1.00 1.00 H ATOM 5859 H62 A D 5 −10.173 33.081 −9.832 1.00 1.00 H ATOM 5860 H2 A D 5 −8.076 34.627 −5.980 1.00 1.00 H ATOM 5861 P G D 6 −0.501 31.223 −5.077 1.00 1.00 P ATOM 5862 O1P G D 6 0.585 31.922 −4.324 1.00 1.00 O ATOM 5863 O2P G D 6 −0.113 29.894 −5.590 1.00 1.00 O ATOM 5864 O5* G D 6 −1.854 31.175 −4.280 1.00 1.00 O ATOM 5865 C5* G D 6 −2.056 32.043 −3.145 1.00 1.00 C ATOM 5866 C4* G D 6 −3.564 31.854 −2.696 1.00 1.00 C ATOM 5867 O4* G D 6 −4.398 31.933 −3.906 1.00 1.00 O ATOM 5868 C1* G D 6 −5.693 31.373 −3.599 1.00 1.00 C ATOM 5869 C2* G D 6 −5.387 30.262 −2.601 1.00 1.00 C ATOM 5870 C3* G D 6 −3.891 30.459 −2.163 1.00 1.00 C ATOM 5871 O3* G D 6 −3.636 30.171 −0.697 1.00 1.00 O ATOM 5872 N9 G D 6 −6.309 30.833 −4.801 1.00 1.00 N ATOM 5873 C8 G D 6 −5.705 30.191 −5.713 1.00 1.00 C ATOM 5874 N7 G D 6 −6.462 29.981 −6.693 1.00 1.00 N ATOM 5875 C5 G D 6 −7.760 30.545 −6.353 1.00 1.00 C ATOM 5876 O6 G D 6 −9.318 30.204 −8.057 1.00 1.00 O ATOM 5877 C6 G D 6 −9.094 30.666 −6.947 1.00 1.00 C ATOM 5878 N1 G D 6 −10.037 31.214 −6.116 1.00 1.00 N ATOM 5879 N2 G D 6 −10.757 32.325 −4.171 1.00 1.00 N ATOM 5880 C2 G D 6 −9.791 31.753 −4.885 1.00 1.00 C ATOM 5881 N3 G D 6 −8.603 31.715 −4.429 1.00 1.00 N ATOM 5882 C4 G D 6 −7.538 31.050 −5.151 1.00 1.00 C ATOM 5883 H5*1 G D 6 −1.957 33.089 −3.429 1.00 1.00 H ATOM 5884 H5*2 G D 6 −1.424 31.804 −2.259 1.00 1.00 H ATOM 5885 H4* G D 6 −3.789 32.688 −1.971 1.00 1.00 H ATOM 5886 H1* G D 6 −6.302 32.186 −3.163 1.00 1.00 H ATOM 5887 H2*1 G D 6 −6.079 30.438 −1.718 1.00 1.00 H ATOM 5888 H2*2 G D 6 −5.560 29.235 −2.929 1.00 1.00 H ATOM 5889 H3* G D 6 −3.222 29.761 −2.689 1.00 1.00 H ATOM 5890 H8 G D 6 −4.665 29.856 −5.507 1.00 1.00 H ATOM 5891 H1 G D 6 −11.000 31.250 −6.505 1.00 1.00 H ATOM 5892 H21 G D 6 −10.535 32.744 −3.284 1.00 1.00 H ATOM 5893 H22 G D 6 −11.698 32.358 −4.598 1.00 1.00 H ATOM 5894 P C D 7 −4.089 28.730 −0.128 1.00 1.00 P ATOM 5895 O1P C D 7 −3.467 28.470 1.188 1.00 1.00 O ATOM 5896 O2P C D 7 −3.689 27.651 −1.082 1.00 1.00 O ATOM 5897 O5* C D 7 −5.652 28.568 0.182 1.00 1.00 O ATOM 5898 C5* C D 7 −6.393 29.034 1.344 1.00 1.00 C ATOM 5899 C4* C D 7 −7.962 29.050 1.204 1.00 1.00 C ATOM 5900 O4* C D 7 −8.319 29.915 0.083 1.00 1.00 O ATOM 5901 C1* C D 7 −9.557 29.417 −0.495 1.00 1.00 C ATOM 5902 C2* C D 7 −9.876 28.134 0.274 1.00 1.00 C ATOM 5903 C3* C D 7 −8.517 27.671 0.923 1.00 1.00 C ATOM 5904 O3* C D 7 −8.644 26.677 1.952 1.00 1.00 O ATOM 5905 N1 C D 7 −9.442 29.021 −1.904 1.00 1.00 N ATOM 5906 C6 C D 7 −8.289 28.552 −2.436 1.00 1.00 C ATOM 5907 C5 C D 7 −8.177 28.153 −3.685 1.00 1.00 C ATOM 5908 N4 C D 7 −9.191 27.831 −5.848 1.00 1.00 N ATOM 5909 C4 C D 7 −9.305 28.172 −4.624 1.00 1.00 C ATOM 5910 N3 C D 7 −10.452 28.557 −4.124 1.00 1.00 N ATOM 5911 O2 C D 7 −11.681 29.094 −2.324 1.00 1.00 O ATOM 5912 C2 C D 7 −10.548 28.951 −2.757 1.00 1.00 C ATOM 5913 H5*1 C D 7 −6.074 30.078 1.474 1.00 1.00 H ATOM 5914 H5*2 C D 7 −6.040 28.514 2.266 1.00 1.00 H ATOM 5915 H4* C D 7 −8.543 29.542 2.074 1.00 1.00 H ATOM 5916 H1* C D 7 −10.263 30.245 −0.340 1.00 1.00 H ATOM 5917 H2*1 C D 7 −10.565 28.330 1.103 1.00 1.00 H ATOM 5918 H2*2 C D 7 −10.366 27.333 −0.366 1.00 1.00 H ATOM 5919 H3* C D 7 −7.942 27.164 0.178 1.00 1.00 H ATOM 5920 H6 C D 7 −7.416 28.456 −1.754 1.00 1.00 H ATOM 5921 H5 C D 7 −7.307 27.713 −4.083 1.00 1.00 H ATOM 5922 H41 C D 7 −9.972 27.886 −6.470 1.00 1.00 H ATOM 5923 H42 C D 7 −8.286 27.480 −6.140 1.00 1.00 H ATOM 5924 P G D 8 −9.568 26.635 3.200 1.00 1.00 P ATOM 5925 O1P G D 8 −9.692 28.018 3.725 1.00 1.00 O ATOM 5926 O2P G D 8 −9.135 25.590 4.197 1.00 1.00 O ATOM 5927 O5* G D 8 −10.921 26.231 2.493 1.00 1.00 O ATOM 5928 C5* G D 8 −12.258 26.666 2.813 1.00 1.00 C ATOM 5929 C4* G D 8 −13.190 26.239 1.669 1.00 1.00 C ATOM 5930 O4* G D 8 −12.582 26.458 0.391 1.00 1.00 O ATOM 5931 C1* G D 8 −12.062 25.178 −0.133 1.00 1.00 C ATOM 5932 C2* G D 8 −13.234 24.273 0.292 1.00 1.00 C ATOM 5933 C3* G D 8 −13.415 24.686 1.794 1.00 1.00 C ATOM 5934 O3* G D 8 −14.783 24.321 2.141 1.00 1.00 O ATOM 5935 N9 G D 8 −11.536 25.186 −1.505 1.00 1.00 N ATOM 5936 C8 G D 8 −10.225 25.235 −1.769 1.00 1.00 C ATOM 5937 N7 G D 8 −10.011 25.198 −2.987 1.00 1.00 N ATOM 5938 C5 G D 8 −11.308 25.042 −3.672 1.00 1.00 C ATOM 5939 O6 G D 8 −10.952 24.971 −6.008 1.00 1.00 O ATOM 5940 C6 G D 8 −11.757 24.943 −5.043 1.00 1.00 C ATOM 5941 N1 G D 8 −13.086 24.742 −5.235 1.00 1.00 N ATOM 5942 N2 G D 8 −15.204 24.472 −4.339 1.00 1.00 N ATOM 5943 C2 G D 8 −13.950 24.736 −4.131 1.00 1.00 C ATOM 5944 N3 G D 8 −13.542 24.931 −2.917 1.00 1.00 N ATOM 5945 C4 G D 8 −12.146 25.066 −2.652 1.00 1.00 C ATOM 5946 H5*1 G D 8 −12.310 27.777 2.830 1.00 1.00 H ATOM 5947 H5*2 G D 8 −12.521 26.310 3.826 1.00 1.00 H ATOM 5948 H4* G D 8 −14.155 26.812 1.742 1.00 1.00 H ATOM 5949 H1* G D 8 −11.254 24.839 0.441 1.00 1.00 H ATOM 5950 H2*1 G D 8 −14.154 24.430 −0.326 1.00 1.00 H ATOM 5951 H2*2 G D 8 −12.906 23.235 0.173 1.00 1.00 H ATOM 5952 H3* G D 8 −12.707 24.199 2.435 1.00 1.00 H ATOM 5953 H8 G D 8 −9.457 25.270 −0.997 1.00 1.00 H ATOM 5954 H1 G D 8 −13.347 24.549 −6.172 1.00 1.00 H ATOM 5955 H21 G D 8 −15.908 24.447 −3.579 1.00 1.00 H ATOM 5956 H22 G D 8 −15.549 24.219 −5.294 1.00 1.00 H ATOM 5957 P C D 9 −15.053 22.849 2.818 1.00 1.00 P ATOM 5958 O1P C D 9 −14.255 21.814 2.101 1.00 1.00 O ATOM 5959 O2P C D 9 −14.813 22.707 4.272 1.00 1.00 O ATOM 5960 O5* C D 9 −16.617 22.548 2.651 1.00 1.00 O ATOM 5961 C5* C D 9 −17.237 22.870 1.412 1.00 1.00 C ATOM 5962 C4* C D 9 −16.580 22.260 0.178 1.00 1.00 C ATOM 5963 O4* C D 9 −16.947 22.838 −1.157 1.00 1.00 O ATOM 5964 C1* C D 9 −16.606 21.891 −2.166 1.00 1.00 C ATOM 5965 C2* C D 9 −17.183 20.631 −1.418 1.00 1.00 C ATOM 5966 C3* C D 9 −16.702 20.701 0.036 1.00 1.00 C ATOM 5967 O3* C D 9 −17.607 20.021 0.911 1.00 1.00 O ATOM 5968 N1 C D 9 −15.239 21.765 −2.737 1.00 1.00 N ATOM 5969 C6 C D 9 −14.138 21.654 −1.946 1.00 1.00 C ATOM 5970 C5 C D 9 −12.946 21.724 −2.530 1.00 1.00 C ATOM 5971 N4 C D 9 −11.517 22.087 −4.433 1.00 1.00 N ATOM 5972 C4 C D 9 −12.691 21.942 −3.916 1.00 1.00 C ATOM 5973 N3 C D 9 −13.763 21.891 −4.642 1.00 1.00 N ATOM 5974 O2 C D 9 −16.019 21.853 −4.875 1.00 1.00 O ATOM 5975 C2 C D 9 −15.089 21.781 −4.072 1.00 1.00 C ATOM 5976 H5*1 C D 9 −17.284 23.934 1.216 1.00 1.00 H ATOM 5977 H5*2 C D 9 −18.288 22.615 1.382 1.00 1.00 H ATOM 5978 H4* C D 9 −15.559 22.664 0.145 1.00 1.00 H ATOM 5979 H1* C D 9 −17.346 21.933 −2.961 1.00 1.00 H ATOM 5980 H2*1 C D 9 −18.248 20.664 −1.382 1.00 1.00 H ATOM 5981 H2*2 C D 9 −16.950 19.727 −1.913 1.00 1.00 H ATOM 5982 H3* C D 9 −15.677 20.303 0.247 1.00 1.00 H ATOM 5983 H6 C D 9 −14.037 21.495 −0.871 1.00 1.00 H ATOM 5984 H5 C D 9 −12.014 21.625 −1.914 1.00 1.00 H ATOM 5985 H41 C D 9 −11.405 22.255 −5.455 1.00 1.00 H ATOM 5986 H42 C D 9 −10.697 21.958 −3.804 1.00 1.00 H ATOM 5987 P C D 10 −17.498 18.423 0.975 1.00 1.00 P ATOM 5988 O1P C D 10 −18.258 17.779 2.068 1.00 1.00 O ATOM 5989 O2P C D 10 −16.209 18.275 1.701 1.00 1.00 O ATOM 5990 O5* C D 10 −17.474 17.680 −0.436 1.00 1.00 O ATOM 5991 C5* C D 10 −18.648 17.405 −1.205 1.00 1.00 C ATOM 5992 C4* C D 10 −18.255 16.860 −2.583 1.00 1.00 C ATOM 5993 O4* C D 10 −17.581 17.887 −3.352 1.00 1.00 O ATOM 5994 C1* C D 10 −16.671 17.195 −4.300 1.00 1.00 C ATOM 5995 C2* C D 10 −16.917 15.672 −3.994 1.00 1.00 C ATOM 5996 C3* C D 10 −17.342 15.612 −2.542 1.00 1.00 C ATOM 5997 O3* C D 10 −18.058 14.441 −2.227 1.00 1.00 O ATOM 5998 N1 C D 10 −15.316 17.633 −4.129 1.00 1.00 N ATOM 5999 C6 C D 10 −14.853 17.945 −2.906 1.00 1.00 C ATOM 6000 C5 C D 10 −13.599 18.351 −2.744 1.00 1.00 C ATOM 6001 N4 C D 10 −11.430 18.804 −3.750 1.00 1.00 N ATOM 6002 C4 C D 10 −12.671 18.387 −3.869 1.00 1.00 C ATOM 6003 N3 C D 10 −13.092 18.023 −4.992 1.00 1.00 N ATOM 6004 O2 C D 10 −14.761 17.356 −6.302 1.00 1.00 O ATOM 6005 C2 C D 10 −14.461 17.630 −5.138 1.00 1.00 C ATOM 6006 H5*1 C D 10 −19.258 18.283 −1.313 1.00 1.00 H ATOM 6007 H5*2 C D 10 −19.255 16.626 −0.744 1.00 1.00 H ATOM 6008 H4* C D 10 −19.159 16.636 −3.115 1.00 1.00 H ATOM 6009 H1* C D 10 −16.965 17.412 −5.309 1.00 1.00 H ATOM 6010 H2*1 C D 10 −17.775 15.367 −4.585 1.00 1.00 H ATOM 6011 H2*2 C D 10 −16.004 15.085 −4.295 1.00 1.00 H ATOM 6012 H3* C D 10 −16.475 15.656 −1.893 1.00 1.00 H ATOM 6013 H6 C D 10 −15.479 17.869 −2.006 1.00 1.00 H ATOM 6014 H5 C D 10 −13.112 18.633 −1.752 1.00 1.00 H ATOM 6015 H41 C D 10 −10.777 18.733 −4.580 1.00 1.00 H ATOM 6016 H42 C D 10 −11.042 19.096 −2.828 1.00 1.00 H ATOM 6017 P G D 11 −17.342 13.006 −2.163 1.00 1.00 P ATOM 6018 O1P G D 11 −16.496 13.027 −0.907 1.00 1.00 O ATOM 6019 O2P G D 11 −18.397 11.953 −2.074 1.00 1.00 O ATOM 6020 O5* G D 11 −16.404 12.786 −3.421 1.00 1.00 O ATOM 6021 C5* G D 11 −16.969 12.312 −4.704 1.00 1.00 C ATOM 6022 C4* G D 11 −15.888 12.053 −5.821 1.00 1.00 C ATOM 6023 O4* G D 11 −15.143 13.165 −6.222 1.00 1.00 O ATOM 6024 C1* G D 11 −13.890 12.708 −6.638 1.00 1.00 C ATOM 6025 C2* G D 11 −13.905 11.164 −6.407 1.00 1.00 C ATOM 6026 C3* G D 11 −14.949 10.960 −5.378 1.00 1.00 C ATOM 6027 O3* G D 11 −15.741 9.762 −5.361 1.00 1.00 O ATOM 6028 N9 G D 11 −12.932 13.417 −5.795 1.00 1.00 N ATOM 6029 C8 G D 11 −13.106 13.851 −4.547 1.00 1.00 C ATOM 6030 N7 G D 11 −12.068 14.428 −4.123 1.00 1.00 N ATOM 6031 C5 G D 11 −11.042 14.387 −5.163 1.00 1.00 C ATOM 6032 O6 G D 11 −9.082 15.500 −4.573 1.00 1.00 O ATOM 6033 C6 G D 11 −9.652 14.837 −5.422 1.00 1.00 C ATOM 6034 N1 G D 11 −9.098 14.449 −6.570 1.00 1.00 N ATOM 6035 N2 G D 11 −9.123 13.453 −8.574 1.00 1.00 N ATOM 6036 C2 G D 11 −9.790 13.767 −7.512 1.00 1.00 C ATOM 6037 N3 G D 11 −11.008 13.414 −7.350 1.00 1.00 N ATOM 6038 C4 G D 11 −11.702 13.695 −6.123 1.00 1.00 C ATOM 6039 H5*1 G D 11 −17.672 13.025 −5.112 1.00 1.00 H ATOM 6040 H5*2 G D 11 −17.533 11.367 −4.445 1.00 1.00 H ATOM 6041 H4* G D 11 −16.389 11.746 −6.714 1.00 1.00 H ATOM 6042 H1* G D 11 −13.760 12.876 −7.706 1.00 1.00 H ATOM 6043 H2*1 G D 11 −14.203 10.672 −7.391 1.00 1.00 H ATOM 6044 H2*2 G D 11 −12.907 10.870 −6.070 1.00 1.00 H ATOM 6045 H3* G D 11 −14.654 11.258 −4.383 1.00 1.00 H ATOM 6046 H8 G D 11 −14.004 13.823 −3.965 1.00 1.00 H ATOM 6047 H1 G D 11 −8.131 14.794 −6.720 1.00 1.00 H ATOM 6048 H21 G D 11 −9.585 12.905 −9.261 1.00 1.00 H ATOM 6049 H22 G D 11 −8.150 13.722 −8.725 1.00 1.00 H ATOM 6050 P G D 12 −15.163 8.312 −5.126 1.00 1.00 P ATOM 6051 O1P G D 12 −15.735 7.446 −6.208 1.00 1.00 O ATOM 6052 O2P G D 12 −15.593 7.702 −3.827 1.00 1.00 O ATOM 6053 O5* G D 12 −13.587 8.250 −5.257 1.00 1.00 O ATOM 6054 C5* G D 12 −13.099 7.659 −6.443 1.00 1.00 C ATOM 6055 C4* G D 12 −11.527 7.698 −6.443 1.00 1.00 C ATOM 6056 O4* G D 12 −11.057 9.072 −6.557 1.00 1.00 O ATOM 6057 C1* G D 12 −9.716 9.150 −6.104 1.00 1.00 C ATOM 6058 C2* G D 12 −9.446 7.793 −5.431 1.00 1.00 C ATOM 6059 C3* G D 12 −10.813 7.163 −5.160 1.00 1.00 C ATOM 6060 O3* G D 12 −10.865 5.753 −4.931 1.00 1.00 O ATOM 6061 N9 G D 12 −9.502 10.296 −5.215 1.00 1.00 N ATOM 6062 C8 G D 12 −10.333 10.699 −4.320 1.00 1.00 C ATOM 6063 N7 G D 12 −9.912 11.691 −3.691 1.00 1.00 N ATOM 6064 C5 G D 12 −8.618 12.015 −4.172 1.00 1.00 C ATOM 6065 O6 G D 12 −7.654 13.784 −2.998 1.00 1.00 O ATOM 6066 C6 G D 12 −7.543 12.976 −3.890 1.00 1.00 C ATOM 6067 N1 G D 12 −6.420 12.966 −4.673 1.00 1.00 N ATOM 6068 N2 G D 12 −5.287 12.039 −6.388 1.00 1.00 N ATOM 6069 C2 G D 12 −6.329 11.999 −5.670 1.00 1.00 C ATOM 6070 N3 G D 12 −7.242 11.106 −5.899 1.00 1.00 N ATOM 6071 C4 G D 12 −8.476 11.143 −5.151 1.00 1.00 C ATOM 6072 H5*1 G D 12 −13.372 8.291 −7.312 1.00 1.00 H ATOM 6073 H5*2 G D 12 −13.460 6.618 −6.601 1.00 1.00 H ATOM 6074 H4* G D 12 −11.141 7.182 −7.315 1.00 1.00 H ATOM 6075 H1* G D 12 −9.057 9.337 −6.984 1.00 1.00 H ATOM 6076 H2*1 G D 12 −8.848 7.131 −6.094 1.00 1.00 H ATOM 6077 H2*2 G D 12 −8.831 7.933 −4.505 1.00 1.00 H ATOM 6078 H3* G D 12 −11.236 7.777 −4.335 1.00 1.00 H ATOM 6079 H8 G D 12 −11.295 10.174 −4.089 1.00 1.00 H ATOM 6080 H1 G D 12 −5.628 13.545 −4.457 1.00 1.00 H ATOM 6081 H21 G D 12 −5.229 11.417 −7.174 1.00 1.00 H ATOM 6082 H22 G D 12 −4.501 12.670 −6.257 1.00 1.00 H ATOM 6083 H11 G D 12 −10.197 5.671 −4.205 1.00 1.00 H TER HETATM 6084 MG1 MG E 1 −10.966 4.075 −5.574 1.00 1.00 MG TER HETATM 6085 MG1 MG F 1 −8.325 2.204 −3.133 1.00 1.00 MG TER HETATM 6086 X X G 1 −2.975 −10.873 −2.518 1.00 1.00 X TER HETATM 6087 X X H 1 −23.388 −6.544 −22.744 1.00 1.00 X TER HETATM 6088 X X I 1 6.776 −5.202 11.238 1.00 1.00 X CONECT 5659 5676 CONECT 5660 5676 CONECT 5661 5677 CONECT 5662 5679 CONECT 5663 5680 CONECT 5664 5680 CONECT 5665 5681 CONECT 5666 5684 CONECT 5667 5687 CONECT 5668 5687 CONECT 5669 5690 CONECT 5670 5672 5693 CONECT 5671 5682 CONECT 5672 5670 5673 5674 5675 CONECT 5673 5672 CONECT 5674 5672 CONECT 5675 5672 5676 CONECT 5676 5660 5659 5675 5677 CONECT 5677 5661 5676 5678 5681 CONECT 5678 5677 5679 CONECT 5679 5662 5678 5680 5683 CONECT 5680 5679 5664 5663 5681 CONECT 5681 5680 5665 5677 5682 CONECT 5682 5681 5671 CONECT 5683 5679 5684 5692 CONECT 5684 5683 5666 5685 CONECT 5685 5684 5686 CONECT 5686 5685 5688 5692 CONECT 5687 5668 5667 5688 CONECT 5688 5687 5686 5689 CONECT 5689 5688 5690 CONECT 5690 5669 5689 5691 CONECT 5691 5690 5692 CONECT 5692 5683 5686 5691 CONECT 5693 5670 5694 5695 5696 CONECT 5694 5693 CONECT 5695 5693 CONECT 5696 5693 5697 CONECT 5697 5696 5698 5699 5700 CONECT 5698 5697 CONECT 5699 5697 CONECT 5700 5697 END

Due to sortware incompatabilities with negative residue numbering, residues in the model in Table 6 are numbered in column 5 with an extra 1000 added. Since protein numbering convention does not include a zero, residue 1000 given in column 5 of Table 6 would correspond to −1, residue 999 to −2, residue 998 to −3, and so on. In the same light, residue 1001 corresponds to amino acid residue 1, residue 1002 corresponds to amino acid residue 2, and so on.

Those skilled in the art will appreciate that the invention described herein is susceptible to variations and modifications other than those specifically described. It is to be understood that the invention includes all such variations and modifications. The invention also includes all of the steps, features, compositions and compounds referred to or indicated in this specification, individually or collectively, and any and all combinations of any two or more of said steps or features.

BIBLIOGRAPHY

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1. A method for identifying the spatial position of an amino acid adjacent to an amino acid mutation conferring resistance to a DNA polymerase antagonist within a reverse transcriptase domain of a DNA polymerase from a Hepatitis B virus (HBV), said method comprising: comparing the atomic coordinates of a DNA polymerase from an HBV of genotype D as set forth in Table 6 with a mutation selected from the group consisting of: rtA21S, rtA38E, rtY54H, rtN76D, rtL91I, rtF122L, rtY124H, rtT128N, rtQ130P, rtT184G, rtM204V/I, rtS202I, rtH248N, rtY252L, rtS21A, rtN/S/T/I/V53D, rtY54H, rtS57P, rtL91I, rtS116P, rtL122F, rtF122L, rtN124H, rtY124H, rtH126R, rtY126Q, rtT128N, rtP130Q, rtD131N, rtV134D, rtY135C, rtY141Y/F, rtL145M, rtF151T/F, rtL180M, rtA181T, rtS202G, rtI204V, rtK212R, rtL217R, rtS219A, rtI235I/M, rtN236T, rtN238D, sP120T, sM125T, sS126T, sT127A, sT118R, sM133L/M, sM133T, sF134V, sS143S/T, sD144A, sG145A, sW172Stop, sI195M, sS207R, sY225Y/C, spacerL97I, spacerK115R, spacerH116L, spacerL128F, spacerS137G, spacerR139G, spacerF142S, rtA97V, rtH126R, rtS135Y, rtM204I, PreS1 N114D, PreS1 T115S, PreS2 F22L, PreS2 V39A, PreS2 P52L, sL89V, sT118A, sF161L, sE164D, sI195M, sI208T, PreS1 E86Q, PreS1 N91K, PreS2 P41H, sQ30K, sP120T, sL176V, sV194F, rtS21A, rtL122F, rtN124H, rtH126R, rtP130Q, rtD131N, rtY135C, rtN/S/T/I/V53D, rtY126Q, rtS202G, rtI204V, rtI235I/M, sM125T, sT127A, sT118R, sM133T, sF134V, sI195M, sS207R, sY225Y/C, rtG172E, rtG174C, rtP177L, rtL180V, rtT184S, sR160N, sE164D, sF170L, sL175L/S, sQ181E/G/Q, sC/W182Y/STOP, sW196L, sW196S, sW196STOP, sM198I, sW199S, sS204T, sY206N, sS210K, sS210R, sL216STOP, sY255F, rtL77L/F, rtL77L/M/V, rtL80I, rtL80V, rtH90N/H, rtS117S/Y, rt125DELrt128, rtQ125K, rtQ125N, rtY126Q, rtL128L/M, rtT128A, rtL132L/M, rtN134G, rtS137T, rtN139H, rtN139K, rtY141Y/STOP, rtV/G142L, rtL147L/W, rtK149R, rtG153E, rtR153Q, rtW153S, rtW153Q, rtF166L, rtI169L, rtF178F/L, rtI187L, rtI187I/V, rtV191I, rtV191V/I, rtN202S, rtS202S/C, rtS202G, rtS213T, rtV/G214E, rtS219A, rtS219P, rtN/Q238H, rtN/S/H238N/K, rtN/S/H/T238/T/A/S/L, rtR242R/K, rtR242R/S, rtN248H, rtI253A, s118-207, s117-120DEL, sI68I/M, sC69F/L, sL109I/L, sG112R, sS17T, sT118R, sK122R, sT123P, sT126S, sT131N, sN131T, sM133K/M, sM133I, sY/F134S, sC139C/G, sK141E, sD144E, sG145R, rtT128T/I, rtL82M, rtT135C, rtT150A, rtV163I, rtT184S, rtA200V, rtF202V, rtS213T, rtQ215H, rtS219A, rtA222T, rtI224S, rtL229M, rtL235I, rtN238S, rtS78T, rt116DEL122, rtI163V, rtL180V, rtE8A, rtV23I, rtD31D/G, rtY53D, rtV58V/I, rtA/S21T, rtV/I/N/S/T53D, rtV/I/N/S/T53Y, rtS/T/N/H/A54Y/H, PreS2 L11L/A, PreS2 R171, DEL PreS2 18-21, PreS2 T30A, PreS2 N54H, sT13T/A, PreS2 Q1V, PreS2 Q1M, rtH90D, rtL/F108L, rtL157L/M, rtA181V, rtV207I, rtP109S, rtN/H/A/S/Q238K, s181M, sP214Q, sF83S, sL173F, sW199L, sI126T, sK160R, sS174N, sA84V, sS210N, sC69STOP/C, sC76Y, s110V/I, sY134N, sW172STOP/W, K32M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion; N33D/C/Q/E/G/H/mL/K/M/F/P/S/T/W/Y/V/A/R/deletion; P34S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; H35I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; T37W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion; P59S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; K60M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion; F61P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; A62R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion; V63A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; D83C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/deletion; V84A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; S85T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion; A86R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/YV/deletion; Y89V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion; H90I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; I/L91K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/deletion; P177S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; F178P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; L179K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; L180K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; A181R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion; Q183E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion; F183P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; T184W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion; Y203V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion; M204F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion; L235K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; N236D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; T237W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion; P237S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; N238D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; H238I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; A238R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion; S239T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion; Q238E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion; K239M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion; L247K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; N248D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; H248I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; F249P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; M250F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion; G251H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/deletion; and V251A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; and identifying the amino acids that are spatially adjacent to the mutated amino acid.
 2. The method of claim 1, wherein the variant HBV polymerase comprises a mutation at a position selected from the list consisting of: rtA21, rtA38, rtY54, rtN76, rtL91, rtF122, rtY124, rtT128, rtQ130, rtT184, rtM204, rtS202, rtH248, rtY252, rtS21, rtN/S/T/I/V53, rtY54, rtS57, rtL91, rtS116, rtL122, rtF122, rtN124, rtY124 rtH126, rtY126, rtT128N, rtP130, rtD131, rtV134, rtY135, rtY141, rtL145, rtF151, rtL180, rtA181, rtS202, rtI204, rtK212, rtL217, rtS219, rtI235, rtN236, rtN238, sP120, sM125, sS126, sT127, sT118, sM133, sM133, sF134, sS143, sD144, sG145, sW172, sI195, sS207, sY225, spacerL97, spacerK115, spacerH116, spacerL128, spacerS137, spacerR139, spacerF142, rtA97, rtH126, rtS135, rtM204, PreS1 N114, PreS1 T115, PreS2 F22, PreS2 V39, PreS2 P52, sL89, sT118, sF161, sE164, sI195, sI208, PreS1 E86, PreS1 N91, PreS2 P41, sQ30, sP120, sL176, sV194, rtS21, rtL122, rtN124, rtH126, rtP130, rtD131, rtY135, rtN/S/T/I/V53, rtY126, rtS202, rtI204, rtI235, sM125, sT127, sT118, sM133, sF134, sI195, sS207, sY225, rtG172, rtG174, rtP177, rtL180, rtT184, sR160, sE164, sF170, sL175, sQ181, sC/W182, sW196, sW196, sW196, sM198, sW199, sS204, sY206, sS210, sS210, sL216, sY255, rtL77, rtL77, rtL80, rtL80, rtH90, rtS117, rt125, rt128, rtQ125, rtQ125, rtY126Q, rtL128, rtT128, rtL132, rtN134, rtS137, rtN139, rtN139, rtY141, rtV/G142, rtL147, rtK149, rtG153, rtR153, rtW153, rtW153, rtF166, rtI169, rtF178, rtI187, rtI187, rtV191, rtV191, rtN202, rtS202, rtS202, rtS213, rtV/G214, rtS219, rtS219, rtN/Q238, rtN/S/H238, rtN/S/H/T238, rtR242, rtR242, rtN248, rtI253, s118-207, s117-120, sI68, sC69, sL109, sG112, sS17, sT118, sK122, sT123, sT126, sT131, sN131, sM133, sM133, sY/F134, sC139, sK141, sD144, sG145, rtT128, rtL82, rtT135, rtT150, rtV163, rtT184, rtA200, rtF202, rtS213, rtQ215, rtS219, rtA222, rtI224, rtL229, rtL235, rtN238, rtS78, rt116DEL122, rtI163, rtL180, rtE8, rtV23, rtD31, rtY53, rtV58, rtA/S21, rtV/I/N/S/T53, rtV/I/N/S/T53, rtS/T/N/H/A54, PreS2 L11, PreS2 R17, DEL PreS2 18-21, PreS2 T30, PreS2 N54, sT13, PreS2 Q1, PreS2 Q1, rtH90, rtL/F108, rtL157, rtA181, rtV207, rtP109, rtN/H/A/S/Q238, s181, sP214, sF83, sL173, sW199, sI126, sK160, sS174, sA84, sS210, sC69, sC76, si110, sY134 or sW172.
 3. The method of claim 1, wherein the DNA polymerase antagonist is a nucleoside to nucleotide analog and is selected from the group consisting of: ADV, LMV, FCV, FTC, ETV, DAPD, TDF and DXG.
 4. A computer-assisted method to identify a potential HBV DNA polymerase antagonist comprising the steps of: (a) inputting into a progammed computer data comprising atomic co-ordinates of a wild-type HBV polymerase of genotype D as set forth in Table 6; (b) identifying a spatially adjacent amino acid in a variant HBV DNA polymerase, wherein the variant is a mutation selected from the group consisting of: rtA21S, rtA38E, rtY54H, rtN76D, rtL91I, rtF122L, rtY124H, rtT128N, rtQ130P, rtT184G, rtM204V/I, rtS202I, rtH248N, rtY252L, rtS21A, rtN/S/T/I/V53D, rtY54H, rtS57P, rtL91I, rtS116P, rtL122F, rtF122L, rtN124H, rtY124H, rtH126R, rtY126Q, rtT128N, rtP130Q, rtD131N, rtV134D, rtY135C, rtY141Y/F, rtL145M, rtF151T/F, rtL180M, rtA181T, rtS202G, rtI204V, rtK212R, rtL217R, rtS219A, rtI235I/M, rtN236T, rtN238D, sP120T, sM125T, sS126T, sT127A, sT118R, sM133L/M, sM133T, sF134V, sS143S/T, sD144A, sG145A, sW172Stop, sI195M, sS207R, sY225Y/C, spacerL97I, spacerK115R, spacerH116L, spacerL128F, spacerS137G, spacerR139G, spacerF142S, rtA97V, rtH126R, rtS135Y, rtM204I, PreS1 N114D, PreS1 T15S, PreS2 F22L, PreS2 V39A, PreS2 P52L, sL89V, sT118A, sF161L, sE164D, sI195M, sI208T, PreS1 E86Q, PreS1 N91K, PreS2 P41H, sQ30K, sP120T, sL176V, sV194F, rtS21A, rtL122F, rtN124H, rtH126R, rtP13.0Q, rtD131N, rtY135C, rtN/S/T/I/V53D, rtY126Q, rtS202G, rtI204V, rtI235I/M, sM125T, sT127A, sT118R, sM133T, sF134V, sI195M, sS207R, sY225Y/C, rtG172E, rtG174C, rtP177L, rtL180V, rtT184S, sR160N, sE164D, sF170L, sL175L/S, sQ181E/G/Q, sC/W182Y/STOP, sW196L, sW196S, sW196STOP, sM198I, sW199S, sS204T, sY206N, sS210K, sS210R, sL216STOP, sY255F, rtL77L/F, rtL77L/M/V, rtL80I, rtL80V, rtH90N/H, rtS117S/Y, rt125DELrt128, rtQ125K, rtQ125N, rtY126Q, rtL128L/M, rtT128A, rtL132L/M, rtN134G, rtS137T, rtN139H, rtN139K, rtY141Y/STOP, rtV/G142L, rtL147L/W, rtK149R, rtG153E, rtR153Q, rtW153S, rtW153Q, rtF166L, rtI169L, rtF178F/L, rtI187L, rtI187I/V, rtV191I, rtV191V/I, rtN202S, rtS202S/C, rtS202G, rtS213T, rtV/G214E, rtS219A, rtS219P, rtN/Q238H, rtN/S/H238N/K, rtN/S/H/T238/T/A/S/L, rtR242R/K, rtR242R/S, rtN248H, rtI253A, s118-207, s117-120DEL, sI68I/M, sC69F/L, sL109I/L, sG112R, sS17T, sT118R, sK122R, sT123P, sT126S, sT131N, sN131T, sM133K/M, sM133I, sY/F134S, sC139C/G, sK141E, sD144E, sG145R, rtT128T/I, rtL82M, rtT135C, rtT150A, rtV163I, rtT184S, rtA200V, rtF202V, rtS213T, rtQ215H, rtS219A, rtA222T, rtI224S, rtL229M, rtL235I, rtN238S, rtS78T, rt116DEL122, rtI163V, rtL180V, rtE8A, rtV23I, rtD31D/G, rtY53D, rtV58V/I, rtA/S21T, rtV/I/N/S/T53D, rtV/I/N/S/T53Y, rtS/T/N/H/A54Y/H, PreS2 L11L/A, PreS2 R171, DEL PreS2 18-21, PreS2 T30A, PreS2 N54H, sT13T/A, PreS2 Q1V, PreS2 Q1M, rtH90D, rtL/F108L, rtL157L/M, rtA181V, rtV207I, rtP109S, rtN/H/A/S/Q238K, s181M, sP214Q, sF83S, sL173F, sW199L, sI126T, sK160R, sS174N, sA84V, sS210N, sC69STOP/C, sC76Y, si110V/I, sY134N, sW172STOP/W, K32M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion; N33D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; P34S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; H35I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; T37W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion; P59S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; K60M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion; F61P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; A62R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion; V63A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; D83C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/deletion; V84A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; S85T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion; A86R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/YV/deletion; Y89V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion; H901/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; I/L91K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/deletion; P177S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; F178P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; L179K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; L180K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; A181R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion; Q183E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion; F183P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; T184W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion; Y203V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion; M204F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion; L235K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; N236D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; T237W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion; P237S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; N238D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; H238I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; A238R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion; S239T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion; Q238E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion; K239M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion; L247K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; N248D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; H248I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; F249P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; M250F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion; G251H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/deletion; and V251A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; said variant exhibiting resistance to a DNA polymerase antagonist; (c) generating, using computer methods, a set of atomic co-ordinates of a structure that possesses stereochemical complementarity to the atomic co-ordinates defined in (a) or a subset thereof, thereby generating a criteria data set; (d) inputting, using the processor, the criteria data set to a computer database of chemical structures; (e) selecting from the database, using computer methods, chemical structures that are similar to the criteria data set; and (f) outputting the selected chemical structures that are similar to a portion of the criteria data set; wherein the chemical structures are putative antagonists of the HBV polymerases.
 5. The computer-assisted method of claim 4, further comprising the step of obtaining the putative antagonists having a chemical structure selected in steps (e) and (f) and testing the antagonist or the ability to modulate at least one functional activity of an HBV polymerase.
 6. A computer or a software component thereof that produces a three-dimensional representation of a molecule or molecular complex, which comprises a three-dimensional representation of a homolog of the molecule or molecular complex, which comprises a three-dimensional representation of a homolog of the molecule or molecular complex, in which the homolog comprises a domain that has a root mean square deviation from the backbone atoms of the amino acids of not more than 1.5 Å, in which the computer comprises: (a) a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein the data comprises the structure co-ordinates of an HBV polymerase of genotype D as set forth in Table 6; (b) identifying spatially adjacent amino acids in a variant HBV polymerase selected from the group consisting of: rtA21S, rtA38E, rtY54H, rtN76D, rtL91I, rtF122L, rtY124H, rtT128N, rtQ130P, rtT184G, rtM204V/I, rtS202I, rtH248N, rtY252L, rtS21A, rtN/S/T/I/V53D, rtY54H, rtS57P, rtL91I, rtS116P, rtL122F, rtF122L, rtN124H, rtY124H, rtH126R, rtY126Q, rtT128N, rtP130Q, rtD131N, rtV134D, rtY135C, rtY141Y/F, rtL145M, rtF151T/F, rtL180M, rtA181T, rtS202G, rtI204V, rtK212R, rtL217R, rtS219A, rtI235I/M, rtN236T, rtN238D, sP120T, sM125T, sS126T, sT127A, sT118R, sM133L/M, sM133T, sF134V, sS143S/T, sD144A, sG145A, sW172Stop, s1195M, sS207R, sY225Y/C, spacerL97I, spacerK115R, spacerH116L, spacerL128F, spacerS137G, spacerR139G, spacerF142S, rtA97V, rtH126R, rtS135Y, rtM204I, PreS1 N114D, PreS1 T115S, PreS2 F22L, PreS2 V39A, PreS2 P52L, sL89V, sT118A, sF161L, sE164D, sI195M, sI208T, PreS1 E86Q, PreS1 N91K, PreS2 P41H, sQ30K, sP120T, sL176V, sV194F, rtS21A, rtL122F, rtN124H, rtH126R, rtP130Q, rtD131N, rtY135C, rtN/S/T/I/V53D, rtY126Q, rtS202G, rtI204V, rtI235I/M, sM125T, sT127A, sT118R, sM133T, sF134V, sI195M, sS207R, sY225Y/C, rtG172E, rtG174C, rtP177L, rtL180V, rtT184S, sR160N, sE164D, sF170L, sL175L/S, sQ181E/G/Q, sC/W182Y/STOP, sW196L, sW196S, sW196STOP, sM198I, sW199S, sS204T, sY206N, sS210K, sS210R, sL216STOP, sY255F, rtL77L/F, rtL77L/M/V, rtL801, rtL80V, rtH90N/H, rtS117S/Y, rt125DELrt128, rtQ125K, rtQ125N, rtY126Q, rtL128L/M, rtT128A, rtL132L/M, rtN134G, rtS137T, rtN139H, rtN139K, rtY141Y/STOP, rtV/G142L, rtL147L/W, rtK149R, rtG153E, rtR153Q, rtW153S, rtW153Q, rtF166L, rtI169L, rtF178F/L, rtI187L, rtI187I/V, rtV191I, rtV191V/I, rtN202S, rtS202S/C, rtS202G, rtS213T, rtV/G214E, rtS219A, rtS219P, rtN/Q238H, rtN/S/H238N/K, rtN/S/H/T238/T/A/S/L, rtR242R/K, rtR242R/S, rtN248H, rtI253A, s118-207, s117-120DEL, sI68I/M, sC69F/L, sL109I/L, sG112R, sS17T, sT118R, sK122R, sT123P, sT126S, sT131N, sN131T, sM133K/M, sM133I, sY/F134S, sC139C/G, sK141E, sD144E, sG145R, rtT128T/I, rtL82M, rtT135C, rtT150A, rtV163I, rtT184S, rtA200V, rtF202V, rtS213T, rtQ215H, rtS219A, rtA222T, rtI224S, rtL229M, rtL235I, rtN238S, rtS78T, rt116DEL122, rtI163V, rtL180V, rtE8A, rtV23I, rtD31D/G, rtY53D, rtV58V/I, rtA/S21T, rtV/I/N/S/T53D, rtV/I/N/S/T53Y, rtS/T/N/H/A54Y/H, PreS2 L11L/A, PreS2 R171, DEL PreS2 18-21, PreS2 T30A, PreS2 N54H, sT13T/A, PreS2 Q1V, PreS2 Q1M, rtH90D, rtL/F108L, rtL157L/M, rtA181V, rtV207I, rtP109S, rtN/H/A/S/Q238K, s181M, sP214Q, sF83S, sL173F, sW199L, sI126T, sK160R, sS174N, sA84V, sS210N, sC69STOP/C, sC76Y, si110V/I, sY134N, sW172STOP/W, K32M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion; N33D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; P34S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; H35I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; T37W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion; P59S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; K60M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion; F61P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; A62R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion; V63A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; D83C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/deletion; V84A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; S85T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion; A86R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/YV/deletion; Y89V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion; H901/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; I/L91K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/deletion; P177S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; F178P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; L179K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; L180K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; A181R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion; Q183E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion; F183P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; T184W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion; Y203V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion; M204F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion; L235K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; N236D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; T237W/Y/V/A/R/N/D/C/Q/E/G/H/mL/K/M/F/P/S/deletion; P237S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; N238D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; H238I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; A238R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion; S239T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion; Q238E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion; K239M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion; L247K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; N248D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; H248I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; F249P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; M250F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/mL/K/deletion; G251H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/deletion; and V251A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; said DNA polymerase exhibiting resistance to an antagonist; (c) a working memory for storing instructions for processing the machine-readable data; (d) a central-processing unit coupled to the working memory and to the machine-readable data storage medium for processing the machine-readable data into the three-dimensional representation; and (e) a display coupled to the central-processing unit for displaying the three-dimensional representation.
 7. A computer or a software component thereof that determines the structure co-ordinates corresponding to a three-dimensional structure of a molecule or molecular complex comprising an HBV polymerase, said computer comprises: (a) a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, in which the data comprises at least a portion of the structural co-ordinates of a wild-type HBV polymerase as defined in Table 6; (b) identifying spatially adjacent amino acid in a variant HBV polymerase ahving a mutation selected from the group consisting of: rtA21S, rtA38E, rtY54H, rtN76D, rtL91I, rtF122L, rtY124H, rtT128N, rtQ130P, rtT184G, rtM204V/I, rtS202I, rtH248N, rtY252L, rtS21A, rtN/S/T/I/V53D, rtY54H, rtS57P, rtL91I, rtS116P, rtL122F, rtF122L, rtN124H, rtY124H, rtH126R, rtY126Q, rtT128N, rtP130Q, rtD131N, rtV134D, rtY135C, rtY141Y/F, rtL145M, rtF151T/F, rtL180M, rtA181T, rtS202G, rtI204V, rtK212R, rtL217R, rtS219A, rtI235I/M, rtN236T, rtN238D, sP120T, sM125T, sS126T, sT127A, sT118R, sM133L/M, sM133T, sF134V, sS143S/T, sD144A, sG145A, sW172Stop, sI195M, sS207R, sY225Y/C, spacerL97I, spacerK115R, spacerH116L, spacerL128F, spacerS137G, spacerR139G, spacerF142S, rtA97V, rtH126R, rtS135Y, rtM204I, PreS1 N114D, PreS1 T115S, PreS2 F22L, PreS2 V39A, PreS2 P52L, sL89V, sT118A, sF161L, sE164D, sI195M, sI208T, PreS1 E86Q, PreS1 N91K, PreS2 P41H, sQ30K, sP120T, sL176V, sV194F, rtS21A, rtL122F, rtN124H, rtH126R, rtP130Q, rtD131N, rtY135C, rtN/S/T/I/V53D, rtY126Q, rtS202G, rtI204V, rtI235I/M, sM125T, sT127A, sT118R, sM133T, sF134V, sI195M, sS207R, sY225Y/C, rtG172E, rtG174C, rtP177L, rtL180V, rtT184S, sR160N, sE164D, sF170L, sL175L/S, sQ181E/G/Q, sC/W182Y/STOP, sW196L, sW196S, sW196STOP, sM198I, sW199S, sS204T, sY206N, sS210K, sS210R, sL216STOP, sY255F, rtL77L/F, rtL77L/M/V, rtL80I, rtL80V, rtH90N/H, rtS117S/Y, rt125DELrt128, rtQ125K, rtQ125N, rtY126Q, rtL128L/M, rtT128A, rtL132L/M, rtN134G, rtS137T, rtN139H, rtN139K, rtY141Y/STOP, rtV/G142L, rtL147L/W, rtK149R, rtG153E, rtR153Q, rtW153S, rtW153Q, rtF166L, rtI169L, rtF178F/L, rtI187L, rtI187I/V, rtV191I, rtV191V/I, rtN202S, rtS202S/C, rtS202G, rtS213T, rtV/G214E, rtS219A, rtS219P, rtN/Q238H, rtN/S/H238N/K, rtN/S/H/T238/T/A/S/L, rtR242R/K, rtR242R/S, rtN248H, rtI253A, s118-207, s117-120DEL, sI68I/M, sC69F/L, sL109I/L, sG112R, sS17T, sT118R, sK122R, sT123P, sT126S, sT131N, sN131T, sM133K/M, sM133I, sY/F134S, sC139C/G, sK141E, sD144E, sG145R, rtT128T/I, rtL82M, rtT135C, rtT150A, rtV163I, rtT184S, rtA200V, rtF202V, rtS213T, rtQ215H, rtS219A, rtA222T, rtI224S, rtL229M, rtL235I, rtN238S, rtS78T, rt116DEL122, rtI163V, rtL180V, rtE8A, rtV23I, rtD31D/G, rtY53D, rtV58V/I, rtA/S21T, rtV/I/N/S/T53D, rtV/I/N/S/T53Y, rtS/T/N/H/A54Y/H, PreS2 L11L/A, PreS2 R171, DEL PreS2 18-21, PreS2 T30A, PreS2 N54H, sT13T/A, PreS2 Q1V, PreS2 Q1M, rtH90D, rtL/F108L, rtL157L/M, rtA181V, rtV207I, rtP109S, rtN/H/A/S/Q238K, s181M, sP214Q, sF83S, sL173F, sW199L, sI126T, sK160R, sS174N, sA84V, sS210N, sC69STOP/C, sC76Y, si110V/I, sY134N, sW172STOP/W, K32M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion; N33D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; P34S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; H35I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; T37W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion; P59S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; K60M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion; F61P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; A62R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion; V63A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; D83C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/deletion; V84A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; S85T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion; A86R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/YV/deletion; Y89V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion; H901/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; I/L91K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/deletion; P177S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; F178P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; L179K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; L180K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; A181R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion; Q183E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion; F183P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; T184W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion; Y203V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion; M204F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion; L235K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; N236D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; T237W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion; P237S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; N238D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; H238I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; A238R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion; S239T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion; Q238E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion; K239M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion; L247K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; N248D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; H248I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; F249P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; M250F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion; G251H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/deletion; and V251A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; said variant DNA polymerase exhibiting resistance to an antagonist; (c) a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein the data comprises atomic co-ordinates of differences between the wild type and variant HBV DNA polymerase; (d) a working memory for storing instructions for processing the machine-readable data of (a) and (b) and (c); (e) a central-processing unit coupled to the working memory and to the machine-readable data storage medium of (a) and (b) for performing a transformation of the machine readable data of (a) and for processing the machine-readable data of (b) into structure co-ordinates; and (f) a display coupled to the central-processing unit for displaying the structure co-ordinates of the molecule or molecular complex.
 8. A computer-assisted method to identify or design HBV DNA polymerase antagonists that bind to a domain of HBV polymerase comprising the steps of: (a) inputting into a progammed computer data comprising the atomic co-ordinates of a wild-type HBV polymerase as set forth in Table 6; (b) identifying a spatially adjacent amino acid from a variant HBV DNA polymerase selected from the group consisting of: 28-36, 39-45, 59-66, 69-70, 73-93, 167-184, 198-213, 230-241 and 245-257 and/or at position numbers 4-10, 24-27, 46-58, 67-68, 71-72, 94-120, 165-166, 185-197, 214-227, 242-244 and 258-266; said variant exhibiting resistance to an antagonist; (c) generating, using computer methods, a set of atomic co-ordinates of the variant thereby generating a criteria data set; (d) with a processor, screening a database of chemical strctures that meet the criteria data set; and (e) outputting the selected chemical structures that are similar to the criteria data set.
 9. An antagonist identified by the method of claims 6-8 that interacts with an HBV polymerase.
 10. The antagonist of claim 9, wherein the agent inhibits or reduces the activity of the HBV polymerase.
 11. The antagonist of claim 9, wherein the antagonist is a nucleoside or nucleotide analog.
 12. The antagonist of claim 11, wherein the antagonist is a nucleotide analog.
 13. The antagonist of claim 11, wherein the nucleoside or nucleotide analog is selected from the group consisting of: ADV, LM, FCV, FTC, ETV, DAPD, TDF and DXG.
 14. The antagonist of claim 9, wherein the HBV polymerase comprises a mutation at amino acid residue position numbers selected from the group consisting of: 28-36, 39-45, 59-66, 69-70, 73-93, 167-184, 198-213, 230-241 and 245-257 of the rt domain.
 15. The antagonist of claim 9, wherein the HBV polymerase comprises a mutation at amino acid residue position numbers selected from the group consisting of: 4-10, 24-27, 46-58, 67-68, 71-72, 94-120, 165-166, 185-197, 214-227, 242-244 and 258-266 of the rt domain.
 16. The antagonist of claim 9, wherein the HBV polymerase comprises a mutation at selected from the group consisting of: rtA21S, rtA38E, rtY54H, rtN76D, rtL91I, rtF122L, rtY124H, rtT128N, rtQ130P, rtT184G, rtM204V/I, rtS202I, rtH248N, rtY252L, rtS21A, rtN/S/T/I/V53D, rtY54H, rtS57P, rtL91I, rtS116P, rtL122F, rtF122L, rtN124H, rtY124H, rtH126R, rtY126Q, rtT128N, rtP130Q, rtD131N, rtV134D, rtY135C, rtY141Y/F, rtL145M, rtF151T/F, rtL180M, rtA181T, rtS202G, rtI204V, rtK212R, rtL217R, rtS219A, rtI235I/M, rtN236T, rtN238D, sP120T, sM125T, sS126T, sT127A, sT118R, sM133L/M, sM133T, sF134V, sS143S/T, sD144A, sG145A, sW172Stop, sI195M, sS207R, sY225Y/C, spacerL97I, spacerK115R, spacerH116L, spacerL128F, spacerS137G, spacerR139G, spacerF142S, rtA97V, rtH126R, rtS135Y, rtM204I, PreS1 N114D, PreS1 T15, PreS2 F22L, PreS2 V39A, PreS2 P52L, sL89V, sT118A, sF161L, sE164D, sI195M, sI208T, PreS1 E86Q, PreS1 N91K, PreS2 P41H, sQ30K, sP120T, sL176V, sV194F, rtS21A, rtL122F, rtN124H, rtH126R, rtP130Q, rtD131N, rtY135C, rtN/S/T/I/V53D, rtY126Q, rtS202G, rtI204V, rtI235I/M, sM125T, sT127A, sT118R, sM133T, sF134V, sI195M, sS207R, sY225Y/C, rtG172E, rtG174C, rtP177L, rtL180V, rtT184S, sR160N, sE164D, sF170L, sL175L/S, sQ181E/G/Q, sC/W182Y/STOP, sW196L, sW196S, sW196STOP, sM1981, sW199S, sS204T, sY206N, sS210K, sS210R, sL216STOP, sY255F, rtL77L/F, rtL77L/M/V, rtL80I, rtL80V, rtH90N/H, rtS117S/Y, rt125DELrt128, rtQ125K, rtQ125N, rtY126Q, rtL128L/M, rtT128A, rtL132L/M, rtN134G, rtS137T, rtN139H, rtN139K, rtY141Y/STOP, rtV/G142L, rtL147L/W, rtK149R, rtG153E, rtR153Q, rtW153S, rtW153Q, rtF166L, rtI169L, rtF178F/L, rtI187L, rtI187I/V, rtV191I, rtV191V/I, rtN202S, rtS202S/C, rtS202G, rtS213T, rtV/G214E, rtS219A, rtS219P, rtN/Q238H, rtN/S/H238N/K, rtN/S/H/T238/T/A/S/L, rtR242R/K, rtR242R/S, rtN248H, rtI253A, s118-207, s117-120DEL, sI68I/M, sC69F/L, sL109I/L, sG112R, sS17T, sT118R, sK122R, sT123P, sT126S, sT131N, sN131T, sM133K/M, sM133I, sY/F134S, sC139C/G, sK141E, sD144E, sG145R, rtT128T/I, rtL82M, rtT135C, rtT150A, rtV163I, rtT184S, rtA200V, rtF202V, rtS213T, rtQ215H, rtS219A, rtA222T, rtI224S, rtL229M, rtL235I, rtN238S, rtS78T, rt116DEL122, rtI163V, rtL180V, rtE8A, rtV23I, rtD31D/G, rtY53D, rtV58V/I, rtA/S21T, rtV/I/N/S/T53D, rtV/I/N/S/T53Y, rtS/T/N/H/A54Y/H, PreS2 L11L/A, PreS2 R171, DEL PreS2 18-21, PreS2 T30A, PreS2 N54H, sT13T/A, PreS2 Q1V, PreS2 Q1M, rtH90D, rtL/F108L, rtL157L/M, rtA181V, rtV207I, rtP109S, rtN/H/A/S/Q238K, s181M, sP214Q, sF83S, sL173F, sW199L, sI126T, sK160R, sS174N, sA84V, sS210N, sC69STOP/C, sC76Y, s110V/I, sY134N, sW172STOP/W, K32M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion; N33D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; P34S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; H35V/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; T37W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion; P59S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; K60M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion; F61P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; A62R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion; V63A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; D83C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/deletion; V84A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; S85T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion; A86R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/YV/deletion; Y89V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion; H901/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; I/L91K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/deletion; P177S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; F178P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; L179K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; L180K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; A181R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion; Q183E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion; F183P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; T184W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion; Y203V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion; M204F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion; L235K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; N236D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; T237W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion; P237S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; N238D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; H238I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; A238R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion; S239T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion; Q238E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion; K239M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion; L247K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; N248D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; H248I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; F249P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; M250F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion; G251H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/deletion; and V251A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion.
 17. The antagonist of claim 9, wherein the HBV polymerase comprises a mutation selected from the group consisting of: rtA21, rtA38, rtY54, rtN76, rtL91, rtF122, rtY124, rtT128, rtQ130, rtT184, rtM204, rtS202, rtH248, rtY252, rtS21, rtN/S/T/I/V53, rtY54, rtS57, rtL91, rtS116, rtL122, rtF122, rtN124, rtY124 rtH126, rtY126, rtT128N, rtP130, rtD131, rtV134, rtY135, rtY141, rtL145, rtF151, rtL180, rtA181, rtS202, rtI204, rtK212, rtL217, rtS219, rtI235, rtN236, rtN238, sP120, sM125, sS126, sT127, sT118, sM133, sM133, sF134, sS143, sD144, sG145, sW172, sI195, sS207, sY225, spacerL97, spacerK115, spacerH116, spacerL128, spacerS137, spacerR139, spacerF142, rtA97, rtH126, rtS135, rtM204, PreS1 N114, PreS1 T115, PreS2 F22, PreS2 V39, PreS2 P52, sL89, sT118, sF161, sE164, sI195, sI208, PreS1 E86, PreS1 N91, PreS2 P41, sQ30, sP120, sL176, sV194, rtS21, rtL122, rtN124, rtH126, rtP130, rtD131, rtY135, rtN/S/T/I/V53, rtY126, rtS202, rtI204, rtI235, sM125, sT127, sT118, sM133, sF134, sI195, sS207, sY225, rtG172, rtG174, rtP177, rtL180, rtT184, sR160, sE164, sF170, sL175, sQ181, sC/W182, sW196, sW196, sW196, sM198, sW199, sS204, sY206, sS210, sS210, sL216, sY255, rtL77, rtL77, rtL80, rtL80, rtH90, rtS117, rt125, rt128, rtQ125, rtQ125, rtY126Q, rtL128, rtT128, rtL132, rtN134, rtS137, rtN139, rtN139, rtY141, rtV/G142, rtL147, rtK149, rtG153, rtR153, rtW153, rtW153, rtF166, rtI169, rtF178, rtI187, rtI187, rtV191, rtV191, rtN202, rtS202, rtS202, rtS213, rtV/G214, rtS219, rtS219, rtN/Q238, rtN/S/H238, rtN/S/H/T238, rtR242, rtR242, rtN248, rtI253, s118-207, s117-120, sI68, sC69, sL109, sG112, sS17, sT118, sK122, sT123, sT126, sT131, sN131, sM133, sM133, sY/F134, sC139, sK141, sD144, sG145, rtT128, rtL82, rtT135, rtT150, rtV163, rtT184, rtA200, rtF202, rtS213, rtQ215, rtS219, rtA222, rtI224, rtL229, rtL235, rtN238, rtS78, rt116DEL122, rtI163, rtL180, rtE8, rtV23, rtD31, rtY53, rtV58, rtA/S21, rtV/I/N/S/T53, rtV/I/N/S/T53, rtS/T/N/H/A54, PreS2 L11, PreS2 R17, DEL PreS2 18-21, PreS2 T30, PreS2 N54, sT13, PreS2 Q1, PreS2 Q1, rtH90, rtL/F108, rtL157, rtA181, rtV207, rtP109, rtN/H/A/S/Q238, s181, sP214, sF83, sL173, sW199, sI126, sK160, sS174, sA84, sS210, sC69, sC76, si110, sY134 and sW172.
 18. The antagonist of claim 9, wherein the antagonist is used therapeutically to inhibit HBV replication.
 19. The antagonist of claim 9, wherein the antagonist is used diagnostically.
 20. A composition comprising the antagonist of claim 9, together with one or more pharmaceutically acceptable carriers and/or diluents.
 21. A method of identifying an agent capable of interacting with a variant DNA polymerase or from an HBV resistant to a DNA polymerase antagonist, the variant comprising a mutation selected from the group consisting of: rtA21S, rtA38E, rtY54H, rtN76D, rtL91I, rtF122L, rtY124H, rtT128N, rtQ130P, rtT184G, rtM204V/I, rtS202I, rtH248N, rtY252L, rtS21A, rtN/S/T/I/V53D, rtY54H, rtS57P, rtL91I, rtS116P, rtL122F, rtF122L, rtN124H, rtY124H, rtH126R, rtY126Q, rtT128N, rtP130Q, rtD131N, rtV134D, rtY135C, rtY141Y/F, rtL145M, rtF151T/F, rtL180M, rtA181T, rtS202G, rtI204V, rtK212R, rtL217R, rtS219A, rtI235I/M, rtN236T, rtN238D, sP120T, sM125T, sS126T, sT127A, sT118R, sM133L/M, sM133T, sF134V, sS143S/T, sD144A, sG145A, sW172Stop, sI195M, sS207R, sY225Y/C, spacerL97I, spacerK115R, spacerH116L, spacerL128F, spacerS137G, spacerR139G, spacerF142S, rtA97V, rtH126R, rtS135Y, rtM204I, PreS1 N114D, PreS1 T115S, PreS2 F22L, PreS2 V39A, PreS2 P52L, sL89V, sT118A, sF161L, sE164D, sI195M, sI208T, PreS1 E86Q, PreS1 N91K, PreS2 P41H, sQ30K, sP120T, sL176V, sV194F, rtS21A, rtL122F, rtN124H, rtH126R, rtP130Q, rtD131N, rtY135C, rtN/S/T/I/V53D, rtY126Q, rtS202G, rtI204V, rtI235I/M, sM125T, sT127A, sT118R, sM133T, sF134V, sI195M, sS207R, sY225Y/C, rtG172E, rtG174C, rtP177L, rtL180V, rtT184S, sR160N, sE164D, sF170L, sL175L/S, sQ181E/G/Q, sC/W182Y/STOP, sW196L, sW196S, sW196STOP, sM198I, sW199S, sS204T, sY206N, sS210K, sS210R, sL216STOP, sY255F, rtL77L/F, rtL77L/M/V, rtL80I, rtL80V, rtH90N/H, rtS117S/Y, rt125DELrt128, rtQ125K, rtQ125N, rtY126Q, rtL128L/M, rtT128A, rtL132L/M, rtN134G, rtS137T, rtN139H, rtN139K, rtY141Y/STOP, rtV/G142L, rtL147L/W, rtK149R, rtG153E, rtR153Q, rtW153S, rtW153Q, rtF166L, rtI169L, rtF178F/L, rtI187L, rtI187I/V, rtV191I, rtV191V/I, rtN202S, rtS202S/C, rtS202G, rtS213T, rtV/G214E, rtS219A, rtS219P, rtN/Q238H, rtN/S/H238N/K, rtN/S/H/T238/T/A/S/L, rtR242R/K, rtR242R/S, rtN248H, rtI253A, sI18-207, si17-120DEL, sI68I/M, sC69F/L, sL109I/L, sG112R, sS17T, sT118R, sK122R, sT123P, sT126S, sT131N, sN131T, sM133K/M, sM133I, sY/F134S, sC139C/G, sK141E, sD144E, sG145R, rtT128T/I, rtL82M, rtT135C, rtT150A, rtV163I, rtT184S, rtA200V, rtF202V, rtS213T, rtQ215H, rtS219A, rtA222T, rtI224S, rtL229M, rtL235I, rtN238S, rtS78T, rt116DEL122, rtI163V, rtL180V, rtE8A, rtV23I, rtD31D/G, rtY53D, rtV58V/I, rtA/S21T, rtV/I/N/S/T53D, rtV/I/N/S/T53Y, rtS/T/N/H/A54Y/H, PreS2 L11L/A, PreS2 R171, DEL PreS2 18-21, PreS2 T30A, PreS2 N54H, sT13T/A, PreS2 Q1V, PreS2 Q1M, rtH90D, rtL/F108L, rtL157L/M, rtA181V, rtV207I, rtP109S, rtN/H/A/S/Q238K, s181M, sP214Q, sF83S, sL173F, sW199L, sI126T, sK160R, sS174N, sA84V, sS210N, sC69STOP/C, sC76Y, s1110V/I, sY134N, sW172STOP/W, K32M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion; N33D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; P34S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; H35I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; T37W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion; P59S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; K60M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion; F61P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; A62R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion; V63A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; D83C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/deletion; V84A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; S85T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion; A86R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/YV/deletion; Y89V/A R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion; H901/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; I/L91K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/deletion; P177S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; F178P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; L179K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; L180K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; A181R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/deletion; Q183E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion; F183P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; T184W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion; Y203V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/deletion; M204F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion; L235K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; N236D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; T237W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/deletion; P237S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/deletion; N238D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; H238I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; A238R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/YV/deletion; S239T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/deletion; Q238E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/deletion; K239M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/deletion; L247K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/deletion; N248D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/V/A/R/deletion; H248I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/deletion; F249P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/M/deletion; M250F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/G/H/I/L/K/deletion; G251H/I/L/K/M/F/P/S/T/W/Y/V/A/R/N/D/C/Q/E/deletion; and V251A/R/N/D/C/Q/E/G/H/I/L/K/M/F/P/S/T/W/Y/deletion; the method comprising: (a) mapping a mutation in the variant HBV polymerase to a wild-type HBV DNA polymerase as defined in atomic coordinates as set forth in Table 6; and (b) designing an agent to interact with an HBV DNA polymerase having a chainge in the coordinates.
 22. The method of claim 21, wherein the variant HBV DNA polymerase comprises a mutation at a position selected from the group consisting of: rtA21, rtA38, rtY54, rtN76, rtL91, rtF122, rtY124, rtT128, rtQ130, rtT184, rtM204, rtS202, rtH248, rtY252, rtS21, rtN/S/T/I/V53, rtY54, rtS57, rtL91, rtS116, rtL122, rtF122, rtN124, rtY124 rtH126, rtY126, rtT128N, rtP130, rtD131, rtV134, rtY135, rtY141, rtL145, rtF151, rtL180, rtA181, rtS202, rtI204, rtK212, rtL217, rtS219, rtI235, rtN236, rtN238, sP120, sM125, sS126, sT127, sT118, sM133, sM133, sF134, sS143, sD144, sG145, sW172, sI195, sS207, sY225, spacerL97, spacerK115, spacerH116, spacerL128, spacerS137, spacerR139, spacerF142, rtA97, rtH126, rtS135, rtM204, PreS1 N114, PreS1 T115, PreS2 F22, PreS2 V39, PreS2 P52, sL89, sT118, sF161, sE164, sI195, sI208, PreS1 E86, PreS1 N91, PreS2 P41, sQ30, sP120, sL176, sV194, rtS21, rtL122, rtN124, rtH126, rtP130, rtD131, rtY135, rtN/S/T/I/V53, rtY126, rtS202, rtI204, rtI235, sM125, sT127, sT118, sM133, sF134, sI195, sS207, sY225, rtG172, rtG174, rtP177, rtL180, rtT184, sR160, sE164, sF170, sL175, sQ181, sC/W182, sW196, sW196, sW196, sM198, sW199, sS204, sY206, sS210, sS210, sL216, sY255, rtL77, rtL77, rtL80, rtL80, rtH90, rtS117, rt125, rt128, rtQ125, rtQ125, rtY126Q, rtL128, rtT128, rtL132, rtN134, rtS137, rtN139, rtN139, rtY141, rtV/G142, rtL147, rtK149, rtG153, rtR153, rtW153, rtW153, rtF166, rtI169, rtF178, rtI187, rtI187, rtV191, rtV191, rtN202, rtS202, rtS202, rtS213, rtV/G214, rtS219, rtS219, rtN/Q238, rtN/S/H238, rtN/S/H/T238, rtR242, rtR242, rtN248, rtI253, s118-207, s117-120, sI68, sC69, sL109, sG112, sS17, sT118, sK122, sT123, sT126, sT131, sN131, sM133, sM133, sY/F134, sC139, sK141, sD144, sG145, rtT128, rtL82, rtT135, rtT150, rtV163, rtT184, rtA200, rtF202, rtS213, rtQ215, rtS219, rtA222, rtI224, rtL229, rtL235, rtN238, rtS78, rt116DEL122, rtI163, rtL180, rtE8, rtV23, rtD31, rtY53, rtV58, rtA/S21, rtV/I/N/S/T53, rtV/I/N/S/T53, rtS/T/N/H/A54, PreS2 L11, PreS2 R17, DEL PreS2 18-21, PreS2 T30, PreS2 N54, sT13, PreS2 Q1, PreS2 Q1, rtH90, rtL/F108, rtL157, rtA181, rtV207, rtP109, rtN/H/A/S/Q238, s181, sP214, sF83, sL173, sW199, sI126, sK160, sS174, sA84, sS210, sC69, sC76, si110, sY134 and sW172.
 23. The method of claim 22, wherein the variant HBV DNA polymerase is resistant to a nucleoside or nucleotide analog.
 24. The method of claim 23, wherein the nucleoside or nucleotide analog is selected from the group consisting of: ADV, LM, FCV, FTC, ETV, DAPD, TDF and DXG.
 25. Use of an HBV DNA polymerase comprising amino acid residues selected from the group consisting of: (i) rtE1, rtH12, rtH13, rtH160, rtA162; (ii) rtC-9, rtH-6, rtH90, rtL93, rtH234; and (iii) rtH197, rtC198, rtH216 and rtC213, the amino acid residues defining a metal binding site in the screening of a medicament that inhibits DNA polymerase activity.
 26. The use of claim 25, further comprising amino acid residues 205 and 206 and/or amino acid residue
 33. 27. A method for screening for an agent capable of binding to and/or inhibiting an BHV polymerase, the method comprising: identifying a compound that is capable of binding, associating with or otherwise interacting with a region of an HBV polymerase selected from the group consisting of: (i) rtE1, rtH12, rtH13, rtH160 and rtA162; (ii) rtC-9, rtH-6, rtH90, rtL93, rtH234; and (iii) rtH197, rtC198, rtH216 and rtC213 wherein said region is a metal ion binding site.
 28. The method of claim 27, wherein the agent is further capable of binding to a region of the HBV DNA polymerase defined by amino acid residues 205 and 26 and/or amino acid residue
 83. 29. The method of claim 27, wherein the agent inhibits or reduces the binding of a metal ion to a region or near amino acid residues selected from the group consisting of: (i) rtE1, rtH12, rtH13, rtH160 and rtA162; (ii) rtC-9, rtH-6, rtH90, rtL93, rtH234; and (iii) rtH197, rtC198, rtH216 and rtC213 wherein said region is a metal ion binding site.
 30. The method of claim 27, wherein the agent inhibits or reduces the activity or reduces the activity of HBV polymerase.
 31. An isolated agent identified by the method of claim
 27. 32. A vaccine comprising an agent of claim 27 and one or more pharmaceutically acceptable carriers and/or diluents.
 33. A diagnostic agent comprising a molecule capable of binding, associating with or interacting with a region of an HBV DNA polymerase defined at or near amino acid residues selected from the group consisting of: (i) rtE1, rtH12, rtH13, rtH160 and rtA162; (ii) rtC-9, rtH-6, rtH90, rtL93, rtH234; and (iii) rtH197, rtC198, rtH216 and rtC213, wherein said region is a metal ion binding site.
 34. The diagnostic agent of claim 33 linked or coupled to a reporter molecule.
 35. The diagnostic agent of claim 34, wherein the reporter molecule is or is coupled to an antibody or antigen-binding fragment thereof.
 36. A method of detecting an HBV, the method comprising screening for binding of the diagnostic agent of claim
 33. 